GBPA_VIBC1
ID GBPA_VIBC1 Reviewed; 487 AA.
AC A7N3J0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=VIBHAR_04739;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000790; ABU72648.1; -; Genomic_DNA.
DR RefSeq; WP_011999056.1; NC_009784.1.
DR AlphaFoldDB; A7N3J0; -.
DR SMR; A7N3J0; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR EnsemblBacteria; ABU72648; ABU72648; VIBHAR_04739.
DR KEGG; vha:VIBHAR_04739; -.
DR PATRIC; fig|338187.36.peg.3632; -.
DR OMA; WTFTANH; -.
DR OrthoDB; 1005693at2; -.
DR Proteomes; UP000008152; 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..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT CHAIN 30..487
FT /note="GlcNAc-binding protein A"
FT /id="PRO_1000073696"
FT DOMAIN 30..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"
SQ SEQUENCE 487 AA; 53469 MW; 9E2EFC2BAD45FCD8 CRC64;
MKKLPNKSLI ALALLSVSGA SFGHGYVSAY ENGVAEGRAT LCRVPANDTN EKNTNCGGIE
YEPQSVEGPD GFPETGPRDG KIASAENSLA AALDEQTADR WVKRPIQSGN QHFEWNFTAN
HITKDWKYYI TKADWNPNQP LARDSFDLNP FCVVDGGMVK PPMRVSHLCN VPEREGYQVI
LAVWDVGDTA ASFYNVIDVK FDGDSPVLPD WNQGGQIYPS QDLNVGDSVY TRVFGQNGEN
VSYSTELVID SEELGAANNW SHALATKINQ EQTMLQAGQL NAEGVISPIY GTNPIYLKQG
SGLKNVEIDY KINSTAPEYD LEVYGLESEY IIGDSATQLD LTLEATGDIK TEMTVYNHHH
ESLSSHSAEL SDGQVEAATM TLSKSEPGHH MLVVVVKDQQ GKVIEQNTLD FHLIEEQTPP
PSGEYDFVFP EGLNTYTAGT KVLASDGAVY QCKEFPFSGY CTQWSPSATQ FEPGKGSHWS
EAWNKVN