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GBPA_YEREN
ID   GBPA_YEREN              Reviewed;         494 AA.
AC   Q8GBD4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 72.
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}; Synonyms=chiY;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51871 / WA-314 / Serotype O:8;
RX   PubMed=12654803; DOI=10.1128/iai.71.4.1872-1879.2003;
RA   Iwobi A., Heesemann J., Garcia E., Igwe E., Noelting C., Rakin A.;
RT   "Novel virulence-associated type II secretion system unique to high-
RT   pathogenicity Yersinia enterocolitica.";
RL   Infect. Immun. 71:1872-1879(2003).
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; AJ344214; CAC83040.2; -; Genomic_DNA.
DR   RefSeq; WP_005173861.1; NZ_NBTE02000004.1.
DR   AlphaFoldDB; Q8GBD4; -.
DR   SMR; Q8GBD4; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   KEGG; yew:CH47_34; -.
DR   OrthoDB; 1005693at2; -.
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_0000229728"
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
 
 
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