ID   GBPA_ALIFM              Reviewed;         492 AA.
AC   B5ESR7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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};
GN   OrderedLocusNames=VFMJ11_A0178;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001133; ACH64094.1; -; Genomic_DNA.
DR   RefSeq; WP_012535228.1; NC_011186.1.
DR   AlphaFoldDB; B5ESR7; -.
DR   SMR; B5ESR7; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   EnsemblBacteria; ACH64094; ACH64094; VFMJ11_A0178.
DR   KEGG; vfm:VFMJ11_A0178; -.
DR   HOGENOM; CLU_039396_2_0_6; -.
DR   OMA; WTFTANH; -.
DR   Proteomes; UP000001857; Chromosome II.
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; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   CHAIN           24..492
FT                   /note="GlcNAc-binding protein A"
FT                   /id="PRO_1000188769"
FT   DOMAIN          24..204
FT                   /note="Chitin-binding type-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   DOMAIN          443..484
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
SQ   SEQUENCE   492 AA;  54072 MW;  BF702BC3233910A0 CRC64;
     MNKSSTKTLI ALSMMAVSSG VSAHGYVSET NDGIAGSRAA LCKFPTSDTQ EKNRDCGAVQ
     WEPQSVEGPE GFPEKGPADG QIAGAGLVQF SELNEQTADR WVKRPITAGA QTFEWTFTAN
     HVTRTWKYYM TKQNWNPNAV LTRDSFDLTP FCELEYNMEK PPLYPNTFSH ECIVPEREGY
     QVILAVWDVG DTAAAFYNVI DVKFDGNGGV VDPTWSQGGQ INPTRDLNVG ERVFTRVFDA
     SGENVSLSTE LVIENETQGQ ANNWTHALAT KINKEQQNIG AGQLNDKGEF SPQYGPNPVY
     LKAGSGLKSV EIGYQLETVE PVYHLDIEGL ASEYTIGDSA TELDLSLYAT GDMNVELTVY
     NHGKEALANT NVTLKDGDAK SVVMALSKSE KGHHMLVSRI KNMDGELIKQ DMSDFHLVEE
     AVTPPPSGDF DFVFPEGVKD YKAGTKVLAE DSNVYQCKEF PYSGYCVQWT ETATNFAPGV
     GSDWSMAWDK VN