CAZyme Information: MGYG000002273_03679

Basic Information

• Species: Bacteroides stercorirosoris
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides stercorirosoris
• CAZyme ID: MGYG000002273_03679
• CAZy Family: GH97
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
249	MGYG000002273_29|CGC1	28234.25	5.2075

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002273	6091524	Isolate	China	Asia

• Gene Location: Start: 14887; End: 15636 Strand: -

Full Sequence      

MKLEACPIRGTVTAIPEGKNIPSFYKKYIETEGLYVTSSERVSDEALLKACDIISLMLAK
RPDVKAHMVKMGCHVMVIGKDEATCDLPEFAHICNSPDSIAYWNWRARGFGGAPEDELSA
SCGEENLLALPQDKYTGENILIHEFAHLIHMVGIVGVEPDFNDRLEALWKNAGEKGLWAN
TYALSNKEEYFAECVQSFFNCNRYAEPANGVHNSMNRRVKLKAYDPDMYKLLKEYFYEIE
IPINNEIHK

Enzyme Prediction     

No EC number prediction in MGYG000002273_03679.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd20169	Peptidase_M90_mtfA	2.15e-08	137	236	110	208	Mlc titration factor A (MtfA) is a zinc metallopeptidase (M90 peptidase). This subfamily includes the Mlc Titration Factor A (MtfA; also known as YeeI or DgsA anti-repressor MtfA) which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). It can cleave synthetic substrates of both carboxypeptidases and aminopeptidases, with strongest activity towards the latter. Its biologically relevant substrate has yet to be identified. Although it interacts with the transcription repressor Mlc, it does not cleave it. However, Mlc seems to activate the peptidase activity of MtfA. MtfA is related to the catalytic domain of the anthrax lethal factor which is a zinc-dependent metalloprotease, targeting mitogen-activated protein kinase kinases (MAPKKs), and resulting in apoptosis, as well as the Mop (modulation of pathogenesis) protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
pfam06167	Peptidase_M90	8.12e-08	137	236	146	242	Glucose-regulated metallo-peptidase M90. MtfA (earlier known as YeeI) is a transcription factor A that binds Mlc (make large colonies), itself a repressor of glucose and hence a protein important in regulation of the phosphoenolpyruvate:glucose-phosphotransferase (ptsG) system, the major glucose transporter in E.coli. Mlc is a repressor of ptsG, and MtfA is found to bind and inactivate Mlc with high affinity. The membrane-bound protein EIICBGlc encoded by the ptsG gene is the major glucose transporter in Escherichia coli. MtfA is found to be a glucose-regulated peptidase, whose activity is regulated by binding to Mlc available in the cytoplasm, which in turn has been released from EIICBGlc during times when no glucose is taken up. A physiologically relevant target for this peptidase is not yet known.
cd20170	Peptidase_M90-like	1.06e-04	131	233	112	206	uncharacterized M90 peptidase family-like proteins. This subfamily contains uncharacterized M90 peptidase-like domains, similar to the Mlc Titration Factor A (MtfA) peptidase from Escherichia coli, also known as the YeeI gene product, which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). E. coli MtfA has been shown to have aminopeptidase activity with the presence of a single zinc ion in the active site ligated by two histidines in an HEXXH motif. MtfA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
cd20493	M34_ATLF_C-like	4.39e-04	126	199	106	184	C-terminal catalytically active domain of anthrax toxin lethal factor and similar domains; belongs to peptidase family M34. This subfamily includes the C-terminal catalytic domain of anthrax toxin lethal factor (ATLF; EC 3.4.24.83). ATLF and edema factor are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is secreted by Bacillus anthracis to promote disease virulence through disruption of host signaling pathways. ATLF belongs to peptidase family M34 and has the hallmark metalloprotease motif HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). MKKs are cleaved by ATLF near their N-termini, removing the docking sequence for the downstream cognate mitogen-activated protein kinase. Preferred amino acids around the cleavage site can be denoted BBBBxHxH, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. At its N-terminus, ATLF has a related PABD domain which lacks the hallmark metalloprotease motif HEXXH. This subfamily also includes Bacillus thuringiensis Vip2Ac-like_2 which belongs to the Vip family of proteins that are secreted during the vegetative growth phase.
cd20184	M34_peptidase_like	6.80e-04	134	235	48	131	uncharacterized subfamily of peptidase family M34. Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA; it is comprised of the PABD and an adenylyl cyclase domain. Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. This uncharacterized subfamily includes proteins which have an N-terminal SLH domain, and proteins which may have an N-terminal IG-like domain; these proteins have the hallmark metalloprotease motif HEXXH motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO67738.1	2.45e-169	1	249	660	908
ALJ59247.1	7.77e-168	1	249	660	908
QUT89694.1	1.10e-167	1	249	660	908
AII67306.1	4.79e-157	1	249	659	907
QJR78979.1	4.79e-157	1	249	659	907

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002273_03679.