GBPA_VIBCH
ID GBPA_VIBCH Reviewed; 485 AA.
AC Q9KLD5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=GlcNAc-binding protein A;
DE Flags: Precursor;
GN Name=gbpA; OrderedLocusNames=VC_A0811;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Classical CG842 / Serotype O1;
RX PubMed=16341015; DOI=10.1038/nature04249;
RA Kirn T.J., Jude B.A., Taylor R.K.;
RT "A colonization factor links Vibrio cholerae environmental survival and
RT human infection.";
RL Nature 438:863-866(2005).
CC -!- FUNCTION: Probably interacts with GlcNAc residues. May promote
CC attachment to both epithelial cell surfaces and chitin. This function
CC enhances bacterial colonization in the gastrointestinal tract and may
CC also be important in the environment by augment colonization of
CC chitinous structures, leading to improved survival. Promotes bacterial
CC attachment to, and colonization of, zooplankton in the aquatic
CC ecosystem. {ECO:0000269|PubMed:16341015}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16341015}.
CC Note=Secreted via the type II secretion pathway EPS (extracellular
CC protein secretion).
CC -!- SIMILARITY: Belongs to the GbpA family. {ECO:0000305}.
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DR EMBL; AE003853; AAF96709.1; -; Genomic_DNA.
DR PIR; A82414; A82414.
DR RefSeq; NP_233197.1; NC_002506.1.
DR RefSeq; WP_000744635.1; NZ_LT906615.1.
DR PDB; 2XWX; X-ray; 1.80 A; A/B=24-414.
DR PDBsum; 2XWX; -.
DR AlphaFoldDB; Q9KLD5; -.
DR SMR; Q9KLD5; -.
DR STRING; 243277.VC_A0811; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR PRIDE; Q9KLD5; -.
DR DNASU; 2611865; -.
DR EnsemblBacteria; AAF96709; AAF96709; VC_A0811.
DR GeneID; 57742190; -.
DR KEGG; vch:VC_A0811; -.
DR PATRIC; fig|243277.26.peg.3431; -.
DR eggNOG; COG3397; Bacteria.
DR HOGENOM; CLU_039396_2_0_6; -.
DR OMA; WTFTANH; -.
DR BioCyc; VCHO:VCA0811-MON; -.
DR BRENDA; 1.14.99.54; 15003.
DR Proteomes; UP000000584; 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 1: Evidence at protein level;
KW 3D-structure; Chitin-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..485
FT /note="GlcNAc-binding protein A"
FT /id="PRO_0000229723"
FT DOMAIN 24..201
FT /note="Chitin-binding type-4"
FT DOMAIN 437..478
FT /note="Chitin-binding type-3"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2XWX"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2XWX"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2XWX"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 176..201
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:2XWX"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 337..355
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 386..397
FT /evidence="ECO:0007829|PDB:2XWX"
FT STRAND 402..413
FT /evidence="ECO:0007829|PDB:2XWX"
SQ SEQUENCE 485 AA; 53628 MW; 975D21307B02BCE4 CRC64;
MKKQPKMTAI ALILSGISGL AYGHGYVSAV ENGVAEGRVT LCKFAANGTG EKNTHCGAIQ
YEPQSVEGPD GFPVTGPRDG KIASAESALA AALDEQTADR WVKRPIQAGP QTFEWTFTAN
HVTKDWKYYI TKPNWNPNQP LSRDAFDLNP FCVVEGNMVQ PPKRVSHECI VPEREGYQVI
LAVWDVGDTA ASFYNVIDVK FDGNGPVLPD WNPAGQIIPS MDLSIGDTVY TRVFDNDGEN
PAYRTELKID SETLTKANQW SYALATKINQ TQKQQRAGQL NGDQFVPVYG TNPIYLKEGS
GLKSVEIGYQ IEAPQPEYSL TVSGLAKEYE IGEQPIQLDL TLEAQGEMSA ELTVYNHHQK
PLASWSQAMT DGELKSITLE LSEAKAGHHM LVSRIKDRDG NLQDQQTLDF MLVEPQTPPT
PGDYDFVFPN GLKEYVAGTK VLASDGAIYQ CKPWPYSGYC QQWTSNATQY QPGTGSHWEM
AWDKR