CAZyme Information: MGYG000002549_02659

Basic Information

• Species: Bacteroides caccae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides caccae
• CAZyme ID: MGYG000002549_02659
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
954	MGYG000002549_9|CGC1	108822.11	4.9873

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002549	5479119	Isolate	United States	North America

• Gene Location: Start: 6712; End: 9576 Strand: +

Full Sequence      

MIQYFMKQYLFLLWGITSLIFSSLFLACSDDEPGDKTPVFTIKEEYLQQDFDQKQSSLVI
PVETNLAADAWVVSSNQDWCVAAKDMSGSSPAVKVLVHANEEPDVRSAEITLKSSVQNYT
IQVRQLGYGPAILVKNPNPIIDAAGGPLSIIVTSNIEYTIEQSENSDWIKTVPATRALTD
KEYQYTVDANPYYETRTVTFTYIYTKDDKIRALCSVTQNAKDSGVSDVEIEGDLKISPNG
GKDSEHQPGQGIENSFDGKFGGTPYHSIWNQKANFPVTLEYFFDGTKDIDYLIYHTRSGN
GNFGKLDIYTATEDAPEYTKYGSFDFKMQNASSRVVFAQSLKKATKIKFEVHSGLGDFVS
CDEMEFYQKNPDKKLDAQLLGVFTDITCTEVRDEATDAQINALPGYFANIAIQLKRNTYD
EWEKSFRIQDYHPYSNVEEWAETLMTKRYSNLDNPTGIYVEAGDSVIVLVGDTHGQSLSI
QCIGEEKSGDYVQTAASGETRFLEEGVNKLGFTQRGMLFLMYNTNLQDINAKPVKIHIPL
GSGYVSGFFDVKTDKTNDKYKELINKATYKYFCIRGERIMFYFHRDKMMQAVPYDILSAI
NLWDDIISWQQELMGIDDVRPSQVNNHLFAISPEGSYMWASDYRIGFVYTYLNNILLYDN
VMAAKDNAWGPAHEIGHIHQRAINWPGSTESSNNLFSNYILFKLGKYCSRGSELSALAKA
RFVDKQAWWNMGSATHQNEDTEIHMRMNWQLWNYYHRCGYKTDFWQKLFKLLREDRIVES
NPGAGQLHFAKMASKAANENLTEFFRMWGFLEPVNNVEIEQYGKWNYNVTPTMIAEAVSY
MSQFPAPKHAFYYLEDRKNNDVGIEQYQVGDVGYYTQFKNDQKITKNVTYTRSGQHITIS
SGDEAVAFEVKKGSEIMYFSNFFSFDIPASIPWNDSMKIYAVQANGERKEVKSN

Enzyme Prediction     

No EC number prediction in MGYG000002549_02659.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	2.86e-22	543	809	1	268	Peptidase M60, enhancin and enhancin-like. This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonisation of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
pfam18630	Peptidase_M60_C	4.48e-19	887	948	1	63	Peptidase M60 C-terminal domain. This is C-terminal domain (CTD) of M60-peptidases pfam13402. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerize through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU.
cd14948	BACON	1.57e-13	40	125	2	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
cd14948	BACON	3.75e-09	131	218	1	82	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam13004	BACON	3.98e-07	71	125	3	60	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUU10001.1	0.0	1	954	1	954
AAO79349.1	0.0	26	948	21	854
QQA07622.1	0.0	26	948	21	854
QUT42145.1	0.0	26	948	21	854
QUT69943.1	0.0	26	948	21	854

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KD2_A	1.34e-281	372	948	24	604	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	2.01e-260	420	948	24	556	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
7SCI_A	2.44e-30	380	848	12	477	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
7BLG_A	6.23e-22	231	369	20	162	ChainA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLH_AAAA Chain AAAA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLJ_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLK_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5EV7_A	2.95e-16	408	809	3	379	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000247	0.012112	0.987635	0.000005	0.000009	0.000008

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002549_02659.