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EXUT_ECO57
ID   EXUT_ECO57              Reviewed;         432 AA.
AC   P0AA79; P42609;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Hexuronate transporter {ECO:0000250|UniProtKB:P0AA78};
DE   AltName: Full=Aldohexuronate transport system {ECO:0000250|UniProtKB:P0AA78};
DE   Flags: Precursor;
GN   Name=exuT; OrderedLocusNames=Z4446, ECs3975;
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: Transport of aldohexuronates such as D-glucuronate and D-
CC       galacturonate. {ECO:0000250|UniProtKB:P0AA78}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-
CC         glucuronate(out) + H(+)(out); Xref=Rhea:RHEA:28955,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:142686;
CC         Evidence={ECO:0000250|UniProtKB:P0AA78};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-galacturonate(out) + H(+)(out) = aldehydo-D-
CC         galacturonate(in) + H(+)(in); Xref=Rhea:RHEA:29295,
CC         ChEBI:CHEBI:12952, ChEBI:CHEBI:15378;
CC         Evidence={ECO:0000250|UniProtKB:P0AA78};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AA78}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC       permease family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG58226.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB37398.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG58226.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB37398.1; ALT_INIT; Genomic_DNA.
DR   PIR; F85970; F85970.
DR   PIR; G91125; G91125.
DR   RefSeq; NP_312002.1; NC_002695.1.
DR   RefSeq; WP_001226465.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AA79; -.
DR   SMR; P0AA79; -.
DR   STRING; 155864.EDL933_4315; -.
DR   EnsemblBacteria; AAG58226; AAG58226; Z4446.
DR   EnsemblBacteria; BAB37398; BAB37398; ECs_3975.
DR   GeneID; 58389404; -.
DR   GeneID; 916191; -.
DR   KEGG; ece:Z4446; -.
DR   KEGG; ecs:ECs_3975; -.
DR   PATRIC; fig|386585.9.peg.4149; -.
DR   eggNOG; COG2271; Bacteria.
DR   HOGENOM; CLU_001265_5_1_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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..432
FT                   /note="Hexuronate transporter"
FT                   /id="PRO_0000121380"
FT   TOPO_DOM        33..48
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..99
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..164
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..264
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..293
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..317
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        413..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AA78"
SQ   SEQUENCE   432 AA;  46892 MW;  9C3B2422F2B28ED8 CRC64;
     MRKIKGLRWY MIALVTLGTV LGYLTRNTVA AAAPTLMEEL NISTQQYSYI IAAYSAAYTV
     MQPVAGYVLD VLGTKIGYAM FAVLWAVFCG ATALAGSWGG LAVARGAVGA AEAAMIPAGL
     KASSEWFPAK ERSIAVGYFN VGSSIGAMIA PPLVVWAIVM HSWQMAFIIS GALSFIWAMA
     WLIFYKHPRD QKHLTDEERD YIINGQEAQH QVSTAKKMSV GQILRNRQFW GIALPRFLAE
     PAWGTFNAWI PLFMFKVYGF NLKEIAMFAW MPMLFADLGC ILGGYLPPLF QRWFGVNLIV
     SRKMVVTLGA VLMIGPGMIG LFTNPYVAIM LLCIGGFAHQ ALSGALITLS SDVFGRNEVA
     TANGLTGMSA WLASTLFALV VGALADTIGF SPLFAVLAVF DLLGALVIWT VLQNKPAIEV
     AQETHNDPAP QH
 
 
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