ID   GBPA_VIBPA              Reviewed;         487 AA.
AC   Q87FT0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=VPA1598;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000032; BAC62941.1; -; Genomic_DNA.
DR   RefSeq; NP_801108.1; NC_004605.1.
DR   RefSeq; WP_005480168.1; NC_004605.1.
DR   AlphaFoldDB; Q87FT0; -.
DR   SMR; Q87FT0; -.
DR   STRING; 223926.28810000; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   PRIDE; Q87FT0; -.
DR   EnsemblBacteria; BAC62941; BAC62941; BAC62941.
DR   GeneID; 1192294; -.
DR   KEGG; vpa:VPA1598; -.
DR   PATRIC; fig|223926.6.peg.4518; -.
DR   eggNOG; COG3397; Bacteria.
DR   HOGENOM; CLU_039396_2_0_6; -.
DR   OMA; WTFTANH; -.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01905; GbpA; 1.
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; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Chitin-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   CHAIN           24..487
FT                   /note="GlcNAc-binding protein A"
FT                   /id="PRO_0000229725"
FT   DOMAIN          24..201
FT                   /note="Chitin-binding type-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   DOMAIN          438..479
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   REGION          61..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53630 MW;  243FB0B931BA3E0E CRC64;
     MKSFPNKSLV ALAIASMSSG VLAHGYVSES NDGVAASRAA LCKYPTSDTN ERNTNCGAIQ
     YEPQSVEGPD GFPETGPRDG KIASAETALA AALDEQTADR WVKRPIKSGT QTFEWTFTAN
     HVTRDWKYYI TKPNWNPNAS LSRDSFDLNP FCVVDGNMVQ PPKQMSHQCN VPEREGYHVI
     LAVWDVGDTA ASFYNVIDVK FDGDDPVIPE WTQGGQIIPT MNLKVGDSVY TRVFDQSGEN
     VAYRTELAIS NDVLTQAKNW SYALASKINQ EQTKLQAGQY SEDKFTPVYG TNPIYLQSNS
     GLERVEIGYN IETPVPDYSL TVDGLASEYI IGTEPTALDL TLTAEGDLTA ELTVYNHHRE
     PLASWTGSIQ DGASEQVELT LSKSEPGHHM LVTRIKDTDG NLVDQQTLDF HLKSEEVTPP
     PSGEYDFVFP EGLSSYTAGT KVLASDGAIY QCKPFPYSGY CVQWSESATQ FEPATGSHWE
     MAWDKLN