CAZyme Information: MGYG000000147_03326

Basic Information

• Species: Bacillus paralicheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis
• CAZyme ID: MGYG000000147_03326
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit D

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3596		405472.1	6.0423

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000147	4371304	Isolate	United Kingdom	Europe

• Gene Location: Start: 167081; End: 177871 Strand: -

Full Sequence      

MTKKHEIQDIYPLSYMQEGMLFHTLLNKDTQAYVEQASFSMTGKVDTDIFQKSITALCAR
HDIFRTIFISQNVSVPQQVVLKERTITVEEKDLTHLDRSGQLRLIDDVKKTDRAKGFHLQ
KDGLMRVILFKTGEREFTCIWSFHHIIMDGWCLGIVLKEFFHIYASHLHQTPLKLEPAVP
YGSYIQWLMEQDKEAAARYWEGYLEGYDQQSRLPQQKKAGAKSRQEEVTFSLSKTVTDKL
KELAAKEEVTLSTIFHTLWGMLLQAYNQTDDAVFGSVISGRPAEIAGIERMIGLFINTVP
VRVTGTKVPFVKLIKQVQKDALNGQPYSYHPLYEIQAESAVKQGLIDHILVFENYPVEKE
IALLNSGQDAEDLFRIHDFNMEDETNYSFYLMVAPGENIHLKMRFDSGIHERSFIESVKG
HLQHIIAQVLENPNLTPEELTITTQQEQKDLLSTLKIETKQREYETIQSMFERQAAQSPD
EKAIHYEGQSITYKELNEMANKLARLLRKRGVKRQEPVAIMVERSPALAAGVLGILKAGA
AFVPIDLSHPAERIRYCIENSGCQHIVSQHHVAALAKSAATKRSVTFIEEADAESDGSNV
ETVNTAEDLLYIMYTSGTTGKPKGVLFEHRNMANLLHDQFENSRIDFKTNVLQYASCAFD
VCYQELFTTLLSGGTLCIAPESIKRDPAQLFLLINTQRTEVVFFPTAFVKMLFNEEHYAN
HFPNCVKHVITAGEQLTVSHIFKALLKRHGIHLHNHYGPAETHVVSTCTIHPEGDIPDSP
PIGKPISHNAMYILDKYKRLQPCGVAGELYISGASVGRGYVNNPILTKQKFLPDPFRAGA
VMYRTGDIARLRADGQMDYIGRTDDQVKIRGYRVEPKEIEVTLANHPAVKEAVVLVQKDS
EGEHELCAYYSTRKPIDPSALRHDLADAIPDYMMPVKWTAVPAIPLTANGKVDKSALPEP
TSSASHQSYAAPRNLNELRLSQLWEGLLKRGPVGIRDNFFELGGHSLKATSLISRIAKEW
NVQIPLSDVFAHPTVEGLAAVISETEENPFASIQQIEKKESYPVSSAQKRMYVLHQLDGG
GVSYNIPAVLELTGELDQQRVEAVFRELIRRHEPLRTSFEAGDDGEPVQRIHEKVPFAFS
NESSSESFIRPFDLGKAPLFRAGLATIEKGRYLLLVDMHHIISDGVSIQLLMQEFSELYK
GLELAPLRIQYKDYAAWQETFKTSDIYKRQESYWLKQLAGELPVLELPTDKPRPPAKSFA
GDRVTFEISQELTSRLQQLAGENSCTLYMTLLGIYTVLLSRLSGQEEIIVGSPIAGRPHA
DLESVLGMFVNTLAFRTRPVSGISFKQYLQDIRETALEAYEHQDYPLEKLVDRLGVQREM
SRNPLFDTTFALQNMERQQLSMEGLELRQKDISHPISKFDLSLYMAESGGQIYCQFEYST
DLFERKTIQKWADFFKTLAKNAAQHPELELDHLSILSKKEESALLQNFSPMQKIDFPLDQ
PLHHQLEQQAEKTPDRPAVLADGVSISYRELNERANQIAWKLIGLGIQQEDVIAVMGRRS
PDMLIGIYGILKAGAAYVPIDPDYPEERIRFLMKDSGAKTLLAESNPSMFEGTILPLDGG
RGNHGEAAVNPNLPVPPDALAYIIYTSGSTGRPKGVMVEHRSAVNFLYSLQTRYSLNDSD
IILHKTSYSFDASIWELFWWPFAGASVYLLPQGGEKDPEIILKALEEKEVTAAHFVPSML
HSFLEYMNQRKKPADIRHLKRVFAGGEQLGAHLVSRFHELLPRVELTNSYGPTEATVEAA
YFDVPKRKTLDHVPIGRSGHNMRLYILNKKRQLLPFGCRGELYIAGAGVARGYLNRPELT
EERFLDDPFYSGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAVLRQID
GVREAAVIARTEGEETELCAYIEGQDQQTVRTELRKRLPAYMMPSAFIEMREWPVTPSGK
LDRKALPAPDGAAERRAYTAPQTITEMKLAKLWEEVLKYGPAGIRDHFFEQGGHSLKATA
LVSRIAKAFGVQVPLKEIFAKPTLEELAAVIQELDESPHAAIEPADKQDTYPVSSAQKRM
YVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRI
HDDVPFQLMELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTL
ISEFSELYANRMLASLRIQYKDYAVWQQAFKQGEAYNRQETYWLKQLDGELPVLELPADN
ARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLSRLSGQEDIIIG
SPIAGRPHKDLEPVIGMFVNTLAIRTQPAENKCFSDFLREVRETALEAFEHQDYPFEELV
DRLNVVRDMSRNPLFDAMLVVQNMDRQELFLDGLHIQPADMPQTGAKFDLTLQVSEGDER
IHFRFEYASSLFKQDTIERWASHFTTMLQHIVHAPQTALPAISMLTAKEQQLLMTNFNRM
PEQHGPNITVHELFARQAAKSPSATALITREGVLTYQELDEWSNKIARTLQNQGIGPDLT
VGIMIPKSTGLIAAVLGTWKAGGAYVPIDLEYPDERKQYVLADSGAKLLITDKTAFHQVP
DHFKGEVLLIEDVQEQDTSPILTASGPDHLAYIIYTSGTTGKPKGVMVEHRGVAYTVQWR
STFYEFHDHDIALQLFSISFDAFVTSMFAPLISGVQIVIPAEEEAKDILAIKQYLADYGI
THMNLVPILYRTLLDVLQPEDVQTLRLVTLGGEAIEPNLLERSFSLRPNIEISNEYGPTE
SSITATAARRLKREENVTIGQPIDYTNVYILKGDHLQPIGVTGELCITGPRLARGYINLP
EQTAKVFVQDPFHPDQRMYRTGDLAKWLPDGTLQYVGRMDEQVKIRGYRIEIKEVEAALS
GLAVVKEAAVVDSVTAAGHKELCAYIVVEDGADCGMVRKALAKKVPSYMVPAFFQTLDSL
PTMPNGKLNKPALAKIPHKGETRQTFTAPATDIEKQLAAIWRGVLGVDKIGTDESFFELG
GDSIKALQVSARLHQSGKQLAVKDIFSHPTIQELTPYVRSSQQPISQASVEGEITWSPVQ
KWFLSQNIKEAHHFNQSVMLHRSNPLDEDALRKTLKAITVHHDALRLICAKDEQGNLRLY
NRPANIGEDQLYNLRIFNLTGKPKDHEHIIKHQVRKLQKAMDLENGPLVQAGLFRSSEGD
DLFLAIHHLAVDGISWRIILEDLASGYEQAIRGDDIALPPKTASFQTYTEQLAKYAESRR
LLQQADYWRAIEQHETVALPKEQTHIDKSALKKRNTVSFTFAQQETDAILKDVHNAYNTD
TQDLLLASAALAIWQWVPQKGLKIALEGHGRQSEAADHDISRTVGWFTSIYPVLLQLEPN
TWDDHHEEYMIRTLKTTKDTLRRIPDKGFGYGVLKYMTPPEKAKIEFGKAPDITFNYLGQ
FEIGNRAQTETEQLDAFTFSPLGGGEDITGTWKREQSLDISALVAEGKLTVNITYETGRF
QKETIERLSQDCQYYLRKLMNHCLGKTETEKTVSDFDDRKLTEEALKNITDLLEFH

Enzyme Prediction     

No EC number prediction in MGYG000000147_03326.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19543	DCL_NRPS	0.0	10	433	1	423	DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
cd17655	A_NRPS_Bac	0.0	1507	1990	4	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17656	A_NRPS_ProA	0.0	478	958	1	479	gramicidin S synthase 2, also known as ATP-dependent proline adenylase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd19531	LCL_NRPS-like	0.0	1062	1466	2	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd19531	LCL_NRPS-like	0.0	2090	2495	1	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	543	3102	1	2666
BAY90071.1	5.34e-269	194	3101	312	3286
BAY30132.1	4.07e-267	179	3101	298	3297
BAZ00088.1	1.27e-263	179	3101	298	3295
BAZ75991.1	1.27e-263	179	3101	298	3295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	4.06e-299	1472	3109	177	1808	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A	2.37e-273	1472	3013	177	1712	Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis]
2VSQ_A	1.26e-225	4	1042	6	1039	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	3.54e-212	1060	1986	4	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
5U89_A	3.76e-185	465	1485	24	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	1059	3594	3	2559	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	1	3596	1	3603	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1054	3594	3	2553	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	1054	3589	3	2553	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	1	3594	1	3579	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000053	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000147_03326.