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CADB_ECO57
ID   CADB_ECO57              Reviewed;         444 AA.
AC   P0AAF0; P23891;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cadaverine/lysine antiporter {ECO:0000250|UniProtKB:P0AAE8};
GN   Name=cadB; OrderedLocusNames=Z5735, ECs5114;
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: Under acidic conditions, in the presence of lysine, functions
CC       as a cadaverine:lysine antiporter that facilitates the excretion of
CC       cadaverine and the uptake of lysine. {ECO:0000250|UniProtKB:P0AAE8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cadaverine(in) + L-lysine(out) = cadaverine(out) + L-
CC         lysine(in); Xref=Rhea:RHEA:28895, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:58384; Evidence={ECO:0000250|UniProtKB:P0AAE8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28896;
CC         Evidence={ECO:0000250|UniProtKB:P0AAE8};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AAE8}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC       family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG59332.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38537.1; -; Genomic_DNA.
DR   PIR; B91268; B91268.
DR   RefSeq; NP_313141.1; NC_002695.1.
DR   RefSeq; WP_000092909.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AAF0; -.
DR   SMR; P0AAF0; -.
DR   STRING; 155864.EDL933_5480; -.
DR   EnsemblBacteria; AAG59332; AAG59332; Z5735.
DR   EnsemblBacteria; BAB38537; BAB38537; ECs_5114.
DR   GeneID; 66671956; -.
DR   GeneID; 914165; -.
DR   KEGG; ece:Z5735; -.
DR   KEGG; ecs:ECs_5114; -.
DR   PATRIC; fig|386585.9.peg.5345; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_1_0_6; -.
DR   OMA; FAYDGWL; -.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004754; Amino_acid_antiprt.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   TIGRFAMs; TIGR00905; 2A0302; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..444
FT                   /note="Cadaverine/lysine antiporter"
FT                   /id="PRO_0000054245"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   444 AA;  46665 MW;  E87913B449B0500A CRC64;
     MSSAKKIGLF ACTGVVAGNM MGSGIALLPA NLASIGGIAI WGWIISIIGA MSLAYVYARL
     ATKNPQQGGP IAYAGEISPA FGFQTGVLYY HANWIGNLAI GITAVSYLST FFPVLNDPVP
     AGIACIAIVW VFTFVNMLGG TWVSRLTTIG LVLVLIPVVM TAIVGWHWFD AATYAANWNT
     ADTTDGHAII KSILLCLWAF VGVESAAVST GMVKNPKRTV PLATMLGTGL AGIVYIAATQ
     VLSGMYPSSV MAASGAPFAI SASTILGNWA APLVSAFTAF ACLTSLGSWM MLVGQAGVRA
     ANDGNFPKVY GEVDSNGIPK KGLLLAAVKM TALMILITLM NSAGGKASDL FGELTGIAVL
     LTMLPYFYSC VDLIRFEGVN IRNFVSLICS VLGCVFCFIA LMGASSFELA GTFIVSLIIL
     MFYARKMHER QSHSMDNHTA SNAH
 
 
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