CAZyme Information: MGYG000002357_00406

Basic Information

• Species: Bacillus licheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
• CAZyme ID: MGYG000002357_00406
• CAZy Family: GT2
• CAZyme Description: Surfactin synthase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3585	MGYG000002357_1|CGC5	402133.17	4.8094

Genome Property

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

• Gene Location: Start: 382077; End: 392834 Strand: +

Full Sequence      

MGNTFYPLTHAQRRIWYTEKFYPGTSVSNLSGFGKLKSASGIDSGLLTEAIRKFVRTNDT
MRFRLMFEGEDEPKQYIAEDEPFQIEYFDASESGGADGVLKWGQAEARRPLPLYDSPLFK
FAVVRISEEESWFFAKVHHIISDGISMTILGNRITDIYLKLAKGETDLEPVQSSFTEHIQ
SELEYENSKRFQKDKAYWNAQYEAIPEPVSLKASDTYQIQLDAARFSKEISPDLYKKIQT
YCNEHNISVLSLFLSILHIYMHRVTGQKDVVLGTFMGNRTNAKEKQMLGMFVSTIPMKAS
IEVHQDFSAFVQERMKDQLKIIRHQKYPYNLLINDLRERQPHVSKLFAVSLEYQVMQWQQ
KETVSFLTEPIFSGSEVNDISIHVKERWDTGTLAIDFDYREELFTSEEMAVLYERLMTLL
EDALLSPQKTIAELEIVPAFEKERLLKRASSQTIAYDKNMTLHGLFEQKAADHPEKTAVV
YEGQKLSYRELNEQSSRLAMALRRRGIGPDAPAAIVMERSERVITAMMGVLKAGGAYVPI
DPGFPEERIRFMLEDSKAKAVITDSGLTFETAETVQFSEALSESRENGYPSSAAGAGHLA
YIIYTSGTTGRPKGVMIEHRQVHHLVRGLQQAVGTYDQDDLKLALLAPFHFDASVQQIFT
SLLLGQTLYIVPKKTVSDGRALSDYYRRHQIDVTDGTPAHLQLLAAADDLSGVKLRHMLV
GGEALSRVATERLLQLFAETAESVPAVTNVYGPTETCVDASSFTITNRTDLQYDTAYVPI
GRPIGNNRFYILDENGALLPDGVEGELYIAGDGVGRGYLNLPDMTRDRFLKDPFVSGGLM
YRTGDTARWLPDGTVDFIGRRDDQVKIRGFRIELGEIESVLQGAPAVEKAVVLARHETGG
SLEVCAYVVPKQGGKIHIQGLREHLSKHLPDYMIPSCFVELNEIPLTASGKVDRKALLRH
EVSVSGTAEYAAPRNECEEKMVGIWQEVLGAEQVGIHDQFFDLGGHSLKAMTMLAKIHKA
FGVEVPLQVLFEKPTVAALSGFVSEAEKDGFAVIEPAPESDDYPLSLAQQRIYIVSQLEG
AGVGYNMPAAAMLEGTLDSGRLEAAFQKLIDRHEALRTSFTVVDGEPRQTVHQRVQFKIE
KVKAEGKPIEQIAKSFVRRFDLAKAPLMRAGLVSLADGRHLLLFDMHHLVSDGVSISIIL
NELAALYNGEELPELRLHYKDYAFWQRAQAQEGFQKEEAYWESMFAGELPVLQLMTDEPR
PPVQSFEGDRVSAVLPKDLKEKLAVLAEQNGATLYMVMLSAYNMLLAKYSGQEDVIVGTP
AAGRRHSDLEGIIGMFVNTLAIRSKVDPGRTFADFLNDVKKTVIDAFEHQDYPFERLAEK
FGASRDLSRHPIFDTMFILQNAWEDIPLLGDLHLSIYETNFNIAKFDLTLQAKEEQGELI
LDLDYSTKLFKKDTAERMLKAYLNLLEDMAADPMLRIGEYSLLTEEETNRQLVAFNPATS
DYPREKTIVQLFEEQAAERGGYPALQFEDKVWSYDELNRKANQLARRLRESGVQAGTTAA
ILTARSAEMVIGILAVLKAGGAYVPIDPDHPEKRVQHFFKDSGAAVLLTQKAMKPLAEAA
EFGGDILFVEDENLYMGDASDLRLPISPEAMANLTYTSGTTGTPKGNMVSHRNILRTVKN
ANYLEVMESDIVLSISNYVFDAFMFDVFGSLLNGAKLVIAPKDTILDMSRLAHVLEKEKI
TILMITTALFNLLTDMRPDSLKGLRRVLFGGERASVDHVRRALKTVGRGRLLHMYGPSES
TVFTTYHPVNEVPDDAQAIPIGKPVSNTEVLILDSFSNVQPAGVAGELCVGGDGLVRGYF
NRPELTAEKFTAHPFKTGEKIYRTGDMARWLADGCLEFIGRIDHQVKIRGQRIELGEIEH
HLLTHDMVQEAAVLAVDTGAGDQMICAYFTADQELSSQELRRHAAEGLPGYMIPSVFMQL
DELPLTGNGKIDRRALPEPDIAQAAQKEYTAPRSGTEAQLADLWQEVLNVPKIGVHDNFF
ELGGHSLLGMTLIARIQQEMNVDLQLKDLFQAPTIESLAQAAAKSEKKSAVYIEAAPDRE
TYPVSSAQKRLYVLQQIEGAEKSYNMPAVLQLEGKLDLKRLESAAQMLIKRHEAFCTTFE
IRNGEPVQRIWEAAELTIDVIDADEQEAEKLIKEFIRPFDLTKAPLFRMSIIRVTEEKHL
LLVDMHHIISDGASVSVLIDEMTRLYAGEALEPLRIQYKDYAVWQQHLLTERHKMQEEYW
LKELDGELPVLTLPTDYPRPSVQTFEGSRISFSLKPELVQQLRRLAKETESTLYMVLAAS
YSTFLSKLSGQSEVIFGSPAAGRPHADLSRIIGMFVNTLAIRTRPEGDKPFSAFLEEVKE
TTLGAFEHQDYPFEELIEKLNIQRDMSRNPLFDAVFSMQNADLKDLSMEGVTLKPYDFAH
QTAKFDLTLTAAEEDGLLVFEMEYNTALFKRESIKRWSGYWVNLLEAIAENPDASLSDLS
LLDEADKRRILYEWNETVLDVPQNKTVHELFEAQVLRTPDRGAAVYNGVQWTYKELNARA
NRLARLLIEKGAGPEQRVGIMVKPSLEMAAGVLAILKAGAAYVPIDPGYPAERIGYVLKD
SGAELLLTQSGLTMPDAFTGEVIDLNREASILAGELYPEDDINPSAEAQSDNLAYLIYTS
GTTGQPKGVMVEHQSLVNLCYWHNDAFTVTEQDKSAKYAGFGFDASVWEMFPYWIAGAEL
HIIDEAIRMDITRLNEYFEENGITITFLPTQLCEQFMELDNQSLRVLLTGGDKLKRIEKR
NYTLVNNYGPTENTVVATSTAIDPDEGMLSIGKPIANTRAYVLGQNNEVQPVGVAGELCI
AGRGLARGYLNKPEETAKRFTEDPFVPGERMYRTGDAVKWLEDGRLEYIGRIDQQVKIRG
FRIELSEIEVQLARLSEVQEAVVTDIEDAYGNKALCGYVVADEQLDTESLARKLGQTLPD
YMVPAYWVQLDELPVTANGKVDRRALPQPDVEAQTAEYKAPRTETEQLLADIWQDVLGID
RIGVTDNFFALGGDSIKGIQMASRLQQHGWKLEMKDLFQHPTIGELSAYVQAADDQPIDQ
NPVEGEVTLTPIQRWFFERKFTNEHHWNQSVMLHAPSGFDPEAAGKALTKMIEHHDALRM
VYQRNGNGIVQYNRGLEETAVRPEVIRFNESGAELEAAVLKESNRIQSSINLTEGPLLKA
AIFETDQGDHLLIVIHHLVVDGISWRILLEDFAAGYAQAEKGEPIILQEKTHSFAEYAAR
LKEYARSKAFAKEIGYWQEVEKAETASLPKDDEAEDKRMHHTKTAEFSLSKEETEQLMTK
VHEAYNTEMNDILLTALGLALKEWTGQEDFIICLEGHGREDIMEGLNISRTVGWFTSQFP
ALIQLRHSEDIGYQIKQIKEELRHIPNKGIGYGIYRYLTEEGKKAQPIKHDISFNYLGQF
AEMADSGLFTRSALPSGDPLSPETEKPNALDIVGYIENGILTMSIAYHSLEYKESTVAAV
AASFKTYLLQLIDHCLELDGGELTPSDLGDDELTLEELDKLMEIF

Enzyme Prediction     

No EC number prediction in MGYG000002357_00406.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17651	A_NRPS_VisG_like	0.0	2551	3027	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.
cd19531	LCL_NRPS-like	0.0	2101	2512	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.
cd19531	LCL_NRPS-like	0.0	1062	1473	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.
cd17655	A_NRPS_Bac	0.0	1510	2000	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.
cd17655	A_NRPS_Bac	0.0	465	957	2	486	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	538	3130	1	2679
BAY90071.1	0.0	196	3111	316	3284
BAY30132.1	1.56e-317	196	3111	317	3295
BAZ00088.1	3.69e-317	196	3111	317	3293
BAZ75991.1	3.69e-317	196	3111	317	3293

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	1488	3110	182	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	6.50e-317	1488	3037	182	1723	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]
5U89_A	6.36e-205	1485	2531	4	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6P1J_A	6.69e-204	2100	3026	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]
2VSQ_A	5.23e-196	1061	2079	11	1036	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39845	0.0	1063	3584	6	2557	Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459	0.0	50	3584	53	3599	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1058	3584	5	2551	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P39846	0.0	1055	3582	3	2554	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	6	3584	10	3577	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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002357_00406.