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GBPA_SHEON
ID   GBPA_SHEON              Reviewed;         475 AA.
AC   Q8EHY2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 100.
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=SO_1072;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAN54144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014299; AAN54144.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_716699.1; NC_004347.2.
DR   AlphaFoldDB; Q8EHY2; -.
DR   SMR; Q8EHY2; -.
DR   STRING; 211586.SO_1072; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   PaxDb; Q8EHY2; -.
DR   KEGG; son:SO_1072; -.
DR   PATRIC; fig|211586.12.peg.1029; -.
DR   eggNOG; COG3397; Bacteria.
DR   HOGENOM; CLU_039396_2_0_6; -.
DR   OMA; WTFTANH; -.
DR   OrthoDB; 1005693at2; -.
DR   Proteomes; UP000008186; Chromosome.
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..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   CHAIN           28..475
FT                   /note="GlcNAc-binding protein A"
FT                   /id="PRO_0000229722"
FT   DOMAIN          28..195
FT                   /note="Chitin-binding type-4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
FT   DOMAIN          426..468
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01905"
SQ   SEQUENCE   475 AA;  51191 MW;  B0935D2E34DBAE87 CRC64;
     MPKLTQLSLV TLALTAGSTL VSQTASAHGY VVSPESRSYA CKTGSNVNCG AVQWEPQSVE
     GASGFPESGP ADGKIASAAN GAFSPLDEQS PSRWSKRDIK SGWNDFSWQF TANHVTRNWR
     YYLTRQGWDQ NQPLSRASFD LAPFCVIDGG MVQPPKLVTH NCYVPEDRSG YQVILAVWEV
     GDTTNSFYNA IDVNFSSGAV VPGEWTDIGD INPSLDLKAG DKVMTRVFDA NGEQSAKQTQ
     ITIADATQGA KQNWPFLLAS AINAQQPQLK AGQKNAAGVI SPVYGKNEIF AAPKSGLERV
     EVSFDIAPAP GNQLNVTSLA DDYTIVDGAA QVSFDVSTNA DMQVSAYLFS HDGTAAGYVT
     QAVNNTSASL VLDVVAPKAG HYHLQVKAEP KQGEVIQQNF DLFLKDQATA PDADFIFPEG
     IKSYVAGTKV LQPKTGKVYQ CKPWPYNGYC VQWSPTATGF EPGIGNSWTM AWTEL
 
 
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