CAZyme Information: MGYG000002357_00407

Basic Information

• Species: Bacillus licheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
• CAZyme ID: MGYG000002357_00407
• CAZy Family: GT2
• CAZyme Description: Surfactin synthase subunit 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3588	MGYG000002357_1|CGC5	403059.02	4.9907

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002357	4208157	Isolate	South Korea	Asia

• Gene Location: Start: 392854; End: 403620 Strand: +

Full Sequence      

MGKQKIQKVYPLTPMQEGMLYHAMLDPESSSYFTQLELVIDGEFDLGIFEKSVNQLVRSY
DILRTVFVHQQLQKPRQVVLAERQAIVEFEDLADLDEERQKTRIDRYKQEVQAAGFNLAK
DMLFKTAVFRLDRKKYHLVWSNHHIVMDGWSMGILMKRLFQNYEAFRANRTVPLDQGKPY
ADYIKWLGRQDKDEAASYWEHRLSGLESPSVIPGGKTRPDSGSYRNEEFTFVWDKDMVDA
LQKAANRYHVTAPNLFQAIWGTVLAKYNRSEDVVFGTVVSGRPSEIDGIEHMAGLFINTI
PVRLRVDQNASFAELFKQAQQHAIDAERYDYLPLYEIQKQSALDGRLISHLVAFENYPLD
KELESGTIHERLGFSIKAAGAFEQTNYDFNLIVYPGAEWTIKLKYNGEAFDAAFIEQAAG
HLTRLAEEAIANPESKAGSADMLSKQEQQTLLAFNQTKTGYPREKTIPELFEEQVEASPD
KTAVAADGRSLTYRRLNEKANQLARRLKARGLMHGNAAAIMMERSLEAAVSMLAVLKAGG
VYVPIDPGYPEERIRFLLEDSGAKIVLTKDSPQISLEGYEVLAANAVDAEKEDAANLVHA
NKPGDLAYYIYTSGSTGKPKGVMVEHRNIVRLVKNAGYIPLKSDVKMAQTGAVSFDASTF
EVFGALLNGGTLYPVPKETLLDGKRFRVFLEETGITTMWLTSPLFNQLAQQDPGMFATLN
DLIIGGDALVPGIVNRVKRESPELSLWNGYGPTENTTFSTCFFIDQAYERTIPIGKPIGN
STAYIVDEHGALQPIGVPGELCVGGDGVARGYLNQPELTDEKFVGDPFAEGKRMYRTGDL
AKWLPDGNIEFLGRIDHQVKVRGFRIELGEVEAALARLEGISEAAAVIRENNTGETEICA
YYTAVGARPAAQLRTELSRSLPEYMIPAHLIELDSMPLTANGKVDKRQLPAPIAEETDRF
EAPKNETEKILAAIWEEILGIKQPGIDDNFFSIGGHSLKAMMLTAKIQEQLQKEVPIKVL
FEKPTIRELAEFLQGETKEKTAPIAPAPSRANYPVSSAQRRMYILNQLEEASTSYNVPAV
LLLEGELDKERLEDAFRALISRHETLRTSFELIDGEIVQTIHQDAVFHLTESVADEAEAE
AAIRGFIRPFQLNKAPLVRAELVKLEEKRHLLMIDMHHIITDGSSTGILIRDLASFYHGE
EAPAPKLHYKDFAVWQNGPEHQEKLKEQEQYWLDIFKGELPVLDLPYDFPRPSKRSFEGD
RVVFGINRKLTADVQKLLSEADATLYMFLLAAFNILLSKYASQEDLIVGSPVAGRTHPDL
HNIPGMFVNTLALRNRPEGEKTFKEFLQEVKETSLQGFAKQDYPLEELIEKLPLLRDTSR
NPLFSVFFNMQNMEIPTLKLGDLQISSYSVRHRTAKFDLSLEAVEHDGEIGLSFDYAVSL
FKEETIRRWSGHFLNVIKTICENPGIKLRDIELLSDKERGLLLEEVRRSRAERLEERPFH
VRFEEKAAEMPDQPAVVCGETILTYRGLDERANQIANVLRSEGIGKDDVVGIMLDRSAEV
AAAILGVMKSGGAFLPIDPEMPTSRIQYMLEDSKARWLLTEHSHQAALADWYNGRLIDVR
NDTLMASKKRPHLIHDGASLAYIIYTSGTTGQPKGVQLEHRNLANYVSWFISEARLSASD
KTMLLSSYAFDLGYTSLFPVLLAGGELHIVPKETYTEPETFIHYIGEQGITYIKLTPSLF
HTVVQPQSFALAKGLQSLRLIVLGGEKINPKDVERFHSRYPDTRFINHYGPTETTIGAIA
KPVEPGMIRQFAERPTIGRPISGAGALVLDASRRLVPAGAAGELYITGSGLARGYVNNRE
LTAAKFIENPYTPGTFMYRTGDLVRRLPNGEIEFLGRTDDQVKIRGYRIELKEIEEAFIG
LEHIERAVVLSFTADSGLDELCAYIQAKRQLPVSELRERLSERLPSYMIPSYFVTVDKMP
LAANGKVDRSALPEPQGLSGQSDSYRAPSTEFEKALCGIWEEVLGVRPVGLDDNFFDLGG
HSLKGMMLTSEIQSKLGKKVPLKTLFDCPTAGLLARSIEADGQAEQSGIQPAEKRDWYPV
SSAQQRMYALHHIEKNGTGYNMPSVLMLEGVLDTDRLRRAFADLVNRHETLRTAFVEIDG
CTVQIVHEKADIDLKVIHIHEEDAEAQINRFIRPFDLSTAPLIRAELLSISSARHLLLID
THHIIADGVSRSLFVKEIAQLYKGASLPEPKLHYKDYAVWQQQPDQQENIRKQEDFWLRQ
FKETVPELSLPLDFPRPPVQSFAGDRVHFKVSKGTALKIRRLMAKTNTTLNIVMLAVFNL
FLSRLAGQKDIVVGSAAAGRTNADLKDVPGMFVNSLALKNHVPDQASFSGFLEEVKNNSL
AALDHQDYPFEELIAKLDLPRDMSRNPLFNVMLTTEDPDKETLDLDGLIIKPYETSHAAA
KFDLTLGAFEKDDEIGLQFEYATDLFKKQTIERWSGYLLNLLEAIAENPDASLSDLSLLD
EADKRRILYEWNETVLDVPQNKTVHELFEAQVLRTPDRGAAVYNGVQWTYKELNARANRL
ARLLIEKGAGPEQRVGIMVKPSLEMAAGVLAILKAGAAYVPIDPGYPAERIGYVLKDSGA
ELLLTQSGLTMPDAFTGEVIDLNREASILAGELYPEDDINPSAEAQSDNLAYLIYTSGTT
GQPKGVMVEHQSLVNLCYWHNDAFTVTEQDKSAKYAGFGFDASVWEMFPYWIAGAELHII
DEAIRMDITRLNEYFEENGITITFLPTQLCEQFMELDNQSLRVLLTGGDKLKRIEKRNYT
LVNNYGPTENTVVATSTAIDPDEGMLSIGKPIANTRAYVLGQNNEVQPVGVAGELCIAGR
GLARGYLNKPEETAKRFTEDPFVPGERMYRTGDAVKWLEDGRLEYIGRIDQQVKIRGFRI
ELSEIEVQLARLSEVQEAVVTDIEDAYGNKALCGYVVADEQLDTESLARKLGQTLPDYMV
PAYWVQLDELPVTANGKVDRRALPQPDVEAQTAEYKAPRTETEQLLADIWQDVLGIDRIG
VTDNFFALGGDSIKGIQMASRLQQHGWKLEMKDLFQHPTIGELSSYVQAADAKPIDQGPV
EGEVTLTPIQRWFFERKFTNEHHWNQSVMLHAPSGFDPELVEQTLAALTEHHDALRMVYQ
KNNGRLIQYNRGPDDRSFAFRVVDLRYVTDIETEIAAQANRLQASLDLENGPLVKAEQYQ
TAEGDHLLIVIHHLVIDGVSWRILLEDFASGYSQAAQQHDVVFPDKTNSFKDWAEALEAY
AQTERFLKTADYWRRLEQERICELPKDRAAAERKAENTSAVKFELSEAETRLLLTKVHEP
YGTDINDILLSALSLTIREWTNGSNICINMEGHGREEIIPGMNISRTTGWFTAQYPVVLK
SQAAAGLPETIKNVKETLRRIPDKGIGYGILRYLTDRKKAGAIFSIKPDISFNYLGQIDR
EVQTGFFGPSPYDMGRQVSERSEALYALSFSGIISKEKFILSCSFNTEEYDRQTIQELMD
RFKAFLTALIDHCTAKEEREFTPSDFSAGDLEMEEMGDLFDVLEENLK

Enzyme Prediction     

No EC number prediction in MGYG000002357_00407.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	2546	3027	1	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.
cd19543	DCL_NRPS	0.0	9	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.
cd17651	A_NRPS_VisG_like	0.0	2548	3024	1	491	similar to adenylation domain of virginiamycin S synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. 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.
cd17655	A_NRPS_Bac	0.0	469	952	1	489	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.
cd17655	A_NRPS_Bac	0.0	1502	1995	2	489	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	543	3127	1	2679
BAY30132.1	0.0	180	3108	300	3295
BAY90071.1	0.0	193	3108	312	3284
BAZ00088.1	0.0	180	3108	300	3293
BAZ75991.1	0.0	180	3108	300	3293

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	1490	3107	198	1797	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	5.55e-311	462	1997	202	1717	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	1.23e-242	2	1035	5	1041	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFW_A	1.90e-203	462	1478	202	1205	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	2.19e-202	462	1478	202	1205	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	1049	3585	2	2560	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	6	3583	7	3600	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1053	3585	11	2554	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	1053	3579	11	2553	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	1	3588	1	3583	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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002357_00407.