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POTE_ECOL6
ID   POTE_ECOL6              Reviewed;         439 AA.
AC   P0AAF2; P24170;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putrescine transporter PotE {ECO:0000255|HAMAP-Rule:MF_02073};
DE   AltName: Full=Putrescine-proton symporter / putrescine-ornithine antiporter {ECO:0000255|HAMAP-Rule:MF_02073};
GN   Name=potE {ECO:0000255|HAMAP-Rule:MF_02073}; OrderedLocusNames=c0776;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes both the uptake and excretion of putrescine. The
CC       uptake of putrescine is dependent on the membrane potential and the
CC       excretion involves putrescine-ornithine antiporter activity.
CC       {ECO:0000255|HAMAP-Rule:MF_02073}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out);
CC         Xref=Rhea:RHEA:28891, ChEBI:CHEBI:15378, ChEBI:CHEBI:326268;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine(out) + putrescine(in) = L-ornithine(in) +
CC         putrescine(out); Xref=Rhea:RHEA:28827, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02073};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02073}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02073}.
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:0000255|HAMAP-Rule:MF_02073}.
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DR   EMBL; AE014075; AAN79249.1; -; Genomic_DNA.
DR   RefSeq; WP_000075845.1; NC_004431.1.
DR   AlphaFoldDB; P0AAF2; -.
DR   SMR; P0AAF2; -.
DR   STRING; 199310.c0776; -.
DR   EnsemblBacteria; AAN79249; AAN79249; c0776.
DR   GeneID; 66671040; -.
DR   KEGG; ecc:c0776; -.
DR   eggNOG; COG0531; Bacteria.
DR   HOGENOM; CLU_007946_1_0_6; -.
DR   OMA; AEKVMSV; -.
DR   BioCyc; ECOL199310:C0776-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0015496; F:putrescine:ornithine antiporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_02073; Putrescine_transp; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004754; Amino_acid_antiprt.
DR   InterPro; IPR027566; Symport/antiport_PotE.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   TIGRFAMs; TIGR00905; 2A0302; 1.
DR   TIGRFAMs; TIGR04299; antiport_PotE; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW   Membrane; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..439
FT                   /note="Putrescine transporter PotE"
FT                   /id="PRO_0000054251"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
SQ   SEQUENCE   439 AA;  46495 MW;  C6F800284DA8C5C8 CRC64;
     MSQAKSNKMG VVQLTILTMV NMMGSGIIML PTKLAEVGTI SIISWLVTAV GSMALAWAFA
     KCGMFSRKSG GMGGYAEYAF GKSGNFMANY TYGVSLLIAN VAIAISAVGY GTELLGASLS
     PVQIGLATIG VLWICTVANF GGARITGQIS SITVWGVIIP VVGLCIIGWF WFSPTLYVDS
     WNPHHAPFFS AVGSSIAMTL WAFLGLESAC ANTDVVENPE RNVPIAVLGG TLGAAVIYIV
     STNVIAGIVP NMELANSTAP FGLAFAQMFT PEVGKVIMAL MVMSCCGSLL GWQFTIAQVF
     KSSSDEGYFP KIFSRVTKVD APVQGMLTIV IIQSGLALMT ISPSLNSQFN VLVNLAVVTN
     IIPYILSMAA LVIIQKVANV PPSKAKVANF VAFVGAMYSF YALYSSGEEA MLYGSIVTFL
     GWTLYGLVSP RFELKNKHG
 
 
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