CAZyme Information: MGYG000000012_01077

Basic Information

• Species: Bacillus subtilis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis
• CAZyme ID: MGYG000000012_01077
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit C

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2555	MGYG000000012_1|CGC10	287594.51	5.26

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000012	4053580	Isolate	United Kingdom	Europe

• Gene Location: Start: 1087087; End: 1094754 Strand: -

Full Sequence      

MPQQPEIQDIYPLSFMQEGMLFHSLYDEQSRAYFEQASFTINGQLDLERFQKSMDAVFDR
YDIFRTAFIYKNVAKPRQVVLKQRPCHVHFEDISHLNEKDKEHCTEAFKEQDKSRGFDLQ
TDVLMRISILKWAPDRYVCIWSHHHILMDGWCLGIVIKDFLHIYQALGKGQLPDLPPVQP
YGTYIKWLMQQDREEAAEYWKKRLQHFEKSTPLPKRTDQIPNGTLQQITFTIPEKETAEL
QKIATASGATLNTVFQALWGVMLQKVNRSSDAVFGSVISGRPSELKDVENMVGLFINTIP
IRAQSDSLSFSDLVRRMQKDMNEAEAYSYFPLYDIQAQSALKQELIDHIIVFENTPTQQE
IEKLNQAGSFDFSVKDFEMEEVTNYKCSVKVIPGRTLYVRIHFQTGAYQPSMMSEIEDYL
LHMVSDVISDPSLPVSKMTLLDENKTQKIVSQNNRSVSVSPEAPTLHGLFERQAAFTPER
TAIRFSGGSLTYAELDMYASRLAARLAARGVSKESIVGVLSERSPDMLIAVLAVLKAGGA
YLPLDPEYPEERLSYMLKDSGADLLLTQPGCFAPSFSGETLEVDMSSLAREETERHMSAS
VSGESLAYVIYTSGSTGQPKGVAVEHRQAVSFLTGMQHQFPLSEDDIVMVKTSFSFDASV
WQLFWWSLSGASAYLLPPGWEKDPALIVKAIHQENVTTAHFIPAMLNSFLDQAEIATLGD
GTSLKRVFAGGEPLAPRMAARFTSLLPEVSLIHGYGPTEATVDAAFYVLDPERDRDRLRI
PIGKPVPGARLYVLDPHLAVQPIGVSGELYIAGVGVARGYLNRPALTEERFLEDPFYPGE
RMYKTGDIARWLPDGNMEFLGRTDDQVKIRGYRVEPGEIEAALRSIEGIREAAVTVRTDS
GEPELCAYIEGLPRNEVRAQLERRLPGYMIPAHMIEMEQWPVTPSGKLDRNALPAPNGAA
DAETYTAPRNVTEMKLAQLWEDVLKNGPVGIHDNFFDRGGHSLKATALVSRISKEFDVQV
PLKDVFAHPTIEGLASVIREGTDSPYEAIKPTEQRETYPVSSAQKRIYVLQQLEDGGTGY
NMPAVLELEGKLNPERLDRAFKELINRHESLRTSFEQDGGGEPVQRIHDEVPFTLQTTVL
GDQTEQGAAAAFIKPFDLSQAPLFRAQIVKVSDERHLLLVDMHHIISDGVSVNILIQEFG
KLYNNRTLPALHIQYKDYAVWQEGFKTGDAYQTQEAYWLKQLEGELPVLDLPADQPRPPV
RSFAGDKVSFTLDQDAASGLHKLARENGSTLYMVLLAAYTALLSRLSGQEDIIVGSPIAG
RPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAYEHQDYPFEELVDKLEL
TRDMSRNPLFDVMFVLQNMDQESLDLDELCLKPAANNGHQTSKFDLTLYAQEQPHGLLTF
QMEFSTDLYKKKTIEKWLQYFINMLLSIIQDNKAVLGTINILNEDEAHYLIHELNRTKMD
YPRNETISRLFEMQAEQTPNAIAIVSDTQELTYADLNSWANQIASLLQRKGVGPDRVVAL
LAGRTPELIAGMLGILKAGGAYLPIDSNLPVERIAYMLSDSRAALLLQSEKTEKQLLGIE
CEQIIIEDIQKQGEAKNVESSAGPHSLAYIIYTSGSTGKPKGVMIEQRSVIRLVKNSNYI
TFTPADRLLMTSSIGFDVGSFEFFGPLLNGAALHLSDQQTFLDSQQLKRYIEHQGITTMW
LTSSLFNHLTEQLETTFSQLNHLIIGGEALSASHVNRIRNACPEVSIWNGYGPTENTTFS
TCFHIQKTYELSIPIGRPVGNSSAYILNQWGMLQPAGAVGELCVGGDGVARGYLRRPDLT
KEKFVQNPFVPGDRLYRTGDLARWLPDGTIEYVGRIDDQVKVRGYRVELGEIESALRHID
GVKEAAVLARTGQSGSKELFGYISVKAGTNAEQVRSLLARSLPNYMIPAYIIEMENLPLT
SNGKLNRKALPEPDFASKQTYIPPRNELEEQLALIWQEVLGIQRIGIEDSFFELGGDSIK
ALQVSARLGRHGLSLQVSDLFRHPKIKDLSPFIRKTERVIEQGPVQGDVPWTPIQKWFLS
QDIEERHHFNQSVMLFHTDRLSEDALRASLKKLAEHHDALRMVYRNDGGRWIQINQGIHE
SQLYRLKISDLSQSENDWETQIKREVADLQQSINLQEGPLLHAAWFKTLTGDYLFLAIHH
LVVDGVAWRILLEDLSAGYQQASSGQAIQLPPKTDSYQEYARRIQEYAQSSKLIREEAYW
RSAEEQQTAELPYEMPFHENTDCSKRDSVSFSLSEADTDVLLQNVNHAYSTDTQDILLTA
ASLAICEWTGGSKLRIAMEGHGREHIMPELDISRTVGWFTSMYPALISFENQRDELGTAV
KTVKDTLGRIPNKGIGYGMLKYLTHPENKSIAFSKTPEISFNYLGQFNDIERQGSFRPSS
LGSGKDITHTWKREQIIEISAMAADKKLHFNLSYPPARFHRNTMDQLINRIEHVLLDIMK
HCAGKQKAEKTLSDFSSQSLTAEDLDSISSLVEEL

Enzyme Prediction     

No EC number prediction in MGYG000000012_01077.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19543	DCL_NRPS	0.0	10	431	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.
cd17646	A_NRPS_AB3403-like	0.0	467	953	1	488	Peptide Synthetase. 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.
PRK05691	PRK05691	0.0	6	1039	3253	4309	peptide synthase; Validated
PRK05691	PRK05691	0.0	1	2548	667	3247	peptide synthase; Validated
cd12117	A_NRPS_Srf_like	0.0	1509	1990	1	483	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	7	2087	557	2674
ACX49739.1	8.03e-200	12	1777	11	1846
BAY30132.1	6.82e-193	959	2076	2135	3297
BAY90071.1	1.59e-191	924	2076	2078	3286
BAZ00088.1	1.61e-191	963	2076	2137	3295

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	461	2081	202	1805	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	7.03e-311	461	1994	202	1716	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	4.89e-231	6	1041	8	1042	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.14e-211	1058	1990	6	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	1.37e-192	443	1491	4	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
P39846	0.0	1	2555	1	2560	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P94459	0.0	6	2552	1052	3600	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	1	2070	1	2104	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P39847	0.0	1	2555	1	2555	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	3	2554	1050	3580	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
0.999991	0.000043	0.000002	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000012_01077.