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ZITB_ECO57
ID   ZITB_ECO57              Reviewed;         311 AA.
AC   Q8X400; Q8X3F7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Zinc transporter ZitB;
GN   Name=zitB; OrderedLocusNames=Z0922, ECs0780;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in zinc efflux across the cytoplasmic membrane, thus
CC       reducing zinc accumulation in the cytoplasm and rendering bacteria more
CC       resistant to zinc. It may contribute to zinc homeostasis at low
CC       concentrations of zinc (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55081.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34203.1; -; Genomic_DNA.
DR   PIR; D90726; D90726.
DR   PIR; E85577; E85577.
DR   RefSeq; NP_308807.1; NC_002695.1.
DR   RefSeq; WP_000951313.1; NZ_LPWC02000002.1.
DR   AlphaFoldDB; Q8X400; -.
DR   SMR; Q8X400; -.
DR   STRING; 155864.EDL933_0825; -.
DR   EnsemblBacteria; AAG55081; AAG55081; Z0922.
DR   EnsemblBacteria; BAB34203; BAB34203; ECs_0780.
DR   GeneID; 917515; -.
DR   KEGG; ece:Z0922; -.
DR   KEGG; ecs:ECs_0780; -.
DR   PATRIC; fig|386585.9.peg.899; -.
DR   eggNOG; COG1230; Bacteria.
DR   HOGENOM; CLU_013430_0_0_6; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   Gene3D; 3.30.70.1350; -; 1.
DR   HAMAP; MF_00552; ZitB; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   InterPro; IPR023500; Zn_transptr_ZitB.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF160240; SSF160240; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..311
FT                   /note="Zinc transporter ZitB"
FT                   /id="PRO_0000206108"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..45
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..119
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..2
FT                   /note="MA -> MAHS (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  34468 MW;  2D0F139E0C537587 CRC64;
     MAHSHTSSHL PEDNNARRLL YAFGVTAGFM LVEVIGGFLS GSLALLADAG HMLTDTAALL
     FALLAVQFSR RPPTIRHTFG WLRLTTLAAF VNAIALVVIT ILIVWEAIER FRTPRPVEGG
     MMMAIAVAGL LANILSFWLL HHGSEEKNLN VRAAALHVLG DLLGSVGAII AALIIIWTGW
     TPADPILSIL VSLLVLRSAW RLLKDSVNEL LEGAPVSLDI AELKRRMCRE IPEVRNVHHV
     HVWMVGEKPV MTLHVQVIPP HDHDALLDQI QHYLMDHYQI EHATIQMEYQ PCHGPDCHLN
     EGVSGHSHHH H
 
 
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