CAZyme Information: MGYG000000014_04136

Basic Information

• Species: Clostridium butyricum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum
• CAZyme ID: MGYG000000014_04136
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1060		117411.57	6.3535

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000014	4564499	Isolate	United Kingdom	Europe

• Gene Location: Start: 1965; End: 5147 Strand: -

Full Sequence      

MAEIQREVSSKADALIGLLTNVPKEILDELGYKYQSQDNNLELTILYRGTPEQTKAFIEG
LGGKFQDLGFNFAVVNIPREKLEQLSLSNAIQYIELPKSLYEQDQESNRVSCIAQLAPNF
DVSGEGVLVGFVDSGIDYTHPAFMNTAGTTRIEYIYDLSTGGNIYNKQMIEEAIKSSNPY
SIVPSIDNTGHGTHVAGIACAGGNINPMYRGAAPNASIAMVKAARGTAVLSSQIMQGIKF
LLDRSKELNMPLVINISLSTNDGAHDGSSLLEQYIRTVQSLERVAIVIAAGNEGDAGHHV
GGELTKTQRKIFNIASEEKSIVMNLYKPILPDISINVINPMSQSSGNITIREGYIQGTIG
SNRYDIYVSGPKPFELNSEIKIILSARTGFLAEGVWALEINVLNEYLGEYSIWLPVLEGL
NPATKFLEPNQYNTLGIPATVDNIIAVGSYNYRTNNLSSFSGRGAQNRGNLVKPDLVAPG
EEIVGPVPNGGYDSKTGTSMAAPQVAGICALMMQWGIIKGNDLYLFGQRLKYYLLKGAQR
RRTDVTYPNPLWGYGEVCALNSFNLLQADLNAILSRRYVKQKEVIVTNNTFIEYNIMKKN
IKRKFMNNRSNGNFRADVGGLKIQCFRGDDYIPIDGARITVSGTTGFENVNNIELVTDVV
GLTQIVELPTPPVEYSLDPNINQIPYSLYDLTVERDGFDTVIIRGCQVFPTQIAYQVVNL
ENNLGRGGMRQEVINIPPNTLNGDYPPKIPEDPEKPLPPPTSGVVLPQPIVPEYIIVHQG
VPDDPSAPNYKVPFKDYIKNVASCEIYSTWTNSAIRANIFCIISFTLNRIYTEWYRGKGK
NFDITSSTAYDHAFAYGRNFYDNISQIVDEIFSTYVRRIGRKQPLLTQYCDGKRVSCPEW
LSQWGSQKLGVQGKVPYEILRYYYGNNIELVTAEKVAGSPQSYPGRPLTIGSSGSAVRTI
QSQLNRIARNYPLIPRVAEDGIYGPKTAEAVKTFQQIFGLPQTGVVDYATWYKISDVYVG
VTRIAELTTTESSRIVRQNMFIPPIIPGLDNKRGIPKFYY

Enzyme Prediction     

No EC number prediction in MGYG000000014_04136.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07478	Peptidases_S8_CspA-like	3.79e-176	124	555	3	455	Peptidase S8 family domain in CspA-like proteins. GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07487	Peptidases_S8_1	1.20e-34	124	514	1	245	Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07474	Peptidases_S8_subtilisin_Vpr-like	6.49e-31	124	514	1	251	Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd00306	Peptidases_S8_S53	7.99e-29	127	514	1	224	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
cd07475	Peptidases_S8_C5a_Peptidase	9.90e-26	119	514	5	290	Peptidase S8 family domain in Streptococcal C5a peptidases. Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QES76183.1	2.67e-253	618	1060	1	443
QGH20837.1	3.89e-225	616	1060	2	441
QSX02883.1	3.89e-225	616	1060	2	441
QMW92695.1	3.89e-225	616	1060	2	441
AXB86494.1	3.89e-225	616	1060	2	441

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4I0W_B	2.45e-165	106	566	3	465	Structureof the Clostridium Perfringens CspB protease [Clostridium perfringens],4I0W_D Structure of the Clostridium Perfringens CspB protease [Clostridium perfringens]
6MW4_A	5.77e-50	45	574	7	558	ChainA, Putative germination-specific protease [Clostridioides difficile R20291]
3AFG_A	8.02e-12	119	371	133	356	ChainA, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
4I0W_A	8.46e-11	8	101	1	94	Structureof the Clostridium Perfringens CspB protease [Clostridium perfringens],4I0W_C Structure of the Clostridium Perfringens CspB protease [Clostridium perfringens]
5GL8_A	4.64e-08	339	513	56	235	Thecrystal structure of Nattokinase fragments [Bacillus subtilis subsp. natto],5GL8_B The crystal structure of Nattokinase fragments [Bacillus subtilis subsp. natto]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P15293	4.70e-17	74	531	163	652	PII-type proteinase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=prt PE=3 SV=1
P15292	1.84e-16	74	531	163	652	PIII-type proteinase OS=Lactococcus lactis subsp. cremoris (strain SK11) OX=272622 GN=prtP PE=1 SV=2
P16271	3.13e-16	74	531	163	652	PI-type proteinase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=prtP PE=3 SV=1
Q02470	3.13e-14	74	531	163	652	PII-type proteinase OS=Lacticaseibacillus paracasei OX=1597 GN=prtP PE=1 SV=1
Q5JIZ5	5.35e-11	119	371	156	379	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1

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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000014_04136.