ID   GBPA_ALIF1              Reviewed;         492 AA.
AC   Q5E183;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=VF_A0143;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000021; AAW87213.1; -; Genomic_DNA.
DR   RefSeq; WP_011263042.1; NC_006841.2.
DR   RefSeq; YP_206101.1; NC_006841.2.
DR   AlphaFoldDB; Q5E183; -.
DR   SMR; Q5E183; -.
DR   STRING; 312309.VF_A0143; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   EnsemblBacteria; AAW87213; AAW87213; VF_A0143.
DR   KEGG; vfi:VF_A0143; -.
DR   PATRIC; fig|312309.11.peg.2748; -.
DR   eggNOG; COG3397; Bacteria.
DR   HOGENOM; CLU_039396_2_0_6; -.
DR   OMA; WTFTANH; -.
DR   OrthoDB; 1005693at2; -.
DR   Proteomes; UP000000537; 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; Reference proteome; 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_0000229724"
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;  53976 MW;  0661AF7BE7D81C13 CRC64;
     MNKSSTKTLI ALSMMAVSSG VSAHGYVSET NDGIAGSRAA LCKFPTSDTQ EKNRDCGAVQ
     WEPQSVEGPE GFPEKGPADG QIAGAGLVQF SELNEQTADR WVKRPITAGA QTFEWTFTAN
     HVTRTWKYYM TKQNWNPNAV LTRDSFDLTP FCELEYNMEK PPLYPNTFSH ECIVPEREGY
     QVILAVWDVG DTAAAFYNVI DVKFDGNGGV VDPTWSQGGQ INPTRDLNVG DRVFTRVFDT
     SGENASLSTE LVIENETQGQ ANNWTHALAT KINKEQQNIG AGQLNDKGEF SPQYGSNPVY
     LKAGSGLKSV EIGYQLETVE PVYHLDIEGL ASEYTIGDSA TELDLSLYAT GDMNVELTVY
     NHGKEALANT NVTLKDGEAK SVVMALSKSE KGHHMLVSRI KNMDGELIKQ DMSDFHLVEE
     AVTPPPSGDF DFVFPEGVKG YKAGTKVLAE DGNVYQCKEF PYSGYCVQWT ETATNFAPGV
     GSDWSMAWDK VN