GBPA_YERE8
ID GBPA_YERE8 Reviewed; 494 AA.
AC A1JQE6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=GlcNAc-binding protein A {ECO:0000255|HAMAP-Rule:MF_01905};
DE Flags: Precursor;
GN Name=gbpA {ECO:0000255|HAMAP-Rule:MF_01905}; OrderedLocusNames=YE3576;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Probably interacts with GlcNAc residues. May promote
CC attachment to both epithelial cell surfaces and chitin.
CC {ECO:0000255|HAMAP-Rule:MF_01905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01905}.
CC -!- SIMILARITY: Belongs to the GbpA family. {ECO:0000255|HAMAP-
CC Rule:MF_01905}.
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DR EMBL; AM286415; CAL13602.1; -; Genomic_DNA.
DR RefSeq; WP_005173861.1; NC_008800.1.
DR RefSeq; YP_001007736.1; NC_008800.1.
DR AlphaFoldDB; A1JQE6; -.
DR SMR; A1JQE6; -.
DR STRING; 393305.YE3576; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR PRIDE; A1JQE6; -.
DR EnsemblBacteria; CAL13602; CAL13602; YE3576.
DR KEGG; yen:YE3576; -.
DR PATRIC; fig|393305.7.peg.3799; -.
DR eggNOG; COG3397; Bacteria.
DR HOGENOM; CLU_039396_2_0_6; -.
DR OMA; WTFTANH; -.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR HAMAP; MF_01905; GbpA; 1.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR041029; GbpA_2.
DR InterPro; IPR020879; GlcNAc-bd_A.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF18416; GbpA_2; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 3: Inferred from homology;
KW Chitin-binding; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT CHAIN 22..494
FT /note="GlcNAc-binding protein A"
FT /id="PRO_5000201303"
FT DOMAIN 22..192
FT /note="Chitin-binding type-4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT DOMAIN 435..484
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT REGION 474..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 53425 MW; E85D14542CBFF109 CRC64;
MKLNKIMLAM VVMSISGTAM AHGYIENPPS RNFLCNAQGG SLNKDCGGVQ YEPQSSGETA
DGFPQQGPVD GKLASGDNWV SVNLNQQTAE RWTKVKMKAG PQEFKWKFTA AHPIADFKYY
MTKQDWNPNQ PLTRDSLDLT PFCVIPGGPA STTGSTTHTC NIPERTGYQV IYGAWDVSDT
PGTFYNMIDA EFDGATGEVV VSEWTKSIGN IEPHDDLNAG DTVKLRMFDQ QGERSDLVVE
ITIADAKEGK KNNWSHALAS KLNNTHQDIR AGKKDSKGTV TATHGANAIF INANSNILRA
EVQIEKSPAG EVSATDASFS ANGMKKEYQM ADGALAIHFD VKTMGSMDLE AKVFAADNSV
KGYKDMTLED ASQHVSIAMT GLKAGKHTLV ILGTDAQGKT QQQSIDFMVK GETVKPEVKP
EVKPEVDGAN KQCTAPAWSN KSSYQAKDTV THNGRIYMSK WWADKASVPG DAAVTDTTGN
GSGWGKVWED KGAC