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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
 
 
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