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PROV_ECOLI
ID   PROV_ECOLI              Reviewed;         400 AA.
AC   P14175;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Glycine betaine/proline betaine transport system ATP-binding protein ProV {ECO:0000305};
GN   Name=proV {ECO:0000303|PubMed:2649479}; OrderedLocusNames=b2677, JW2652;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2649479; DOI=10.1128/jb.171.4.1923-1931.1989;
RA   Gowrishankar J.;
RT   "Nucleotide sequence of the osmoregulatory proU operon of Escherichia
RT   coli.";
RL   J. Bacteriol. 171:1923-1931(1989).
RN   [2]
RP   ERRATUM OF PUBMED:2649479.
RA   Gowrishankar J.;
RL   J. Bacteriol. 172:1165-1165(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-224.
RC   STRAIN=K12;
RX   PubMed=2691838; DOI=10.1111/j.1365-2958.1989.tb00253.x;
RA   Stirling D.A., Hulton C.S.J., Waddell L., Park S.F., Stewart G.S.A.B.,
RA   Booth I.R., Higgins C.F.;
RT   "Molecular characterization of the proU loci of Salmonella typhimurium and
RT   Escherichia coli encoding osmoregulated glycine betaine transport
RT   systems.";
RL   Mol. Microbiol. 3:1025-1038(1989).
RN   [7]
RP   FUNCTION IN GLYCINE BETAINE TRANSPORT.
RX   PubMed=3305496; DOI=10.1016/s0021-9258(18)60890-7;
RA   Barron A., Jung J.U., Villarejo W.;
RT   "Purification and characterization of a glycine betaine binding protein
RT   from Escherichia coli.";
RL   J. Biol. Chem. 262:11841-11846(1987).
RN   [8]
RP   FUNCTION IN PROLINE BETAINE TRANSPORT.
RX   PubMed=7898450; DOI=10.1007/bf00290728;
RA   Haardt M., Kempf B., Faatz E., Bremer E.;
RT   "The osmoprotectant proline betaine is a major substrate for the binding-
RT   protein-dependent transport system ProU of Escherichia coli K-12.";
RL   Mol. Gen. Genet. 246:783-786(1995).
RN   [9]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [10]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
RN   [11]
RP   FUNCTION IN GLYCINE BETAINE TRANSPORT, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=23249124; DOI=10.3109/09687688.2012.754060;
RA   Gul N., Poolman B.;
RT   "Functional reconstitution and osmoregulatory properties of the ProU ABC
RT   transporter from Escherichia coli.";
RL   Mol. Membr. Biol. 30:138-148(2013).
CC   -!- FUNCTION: Part of the ProU ABC transporter complex involved in glycine
CC       betaine and proline betaine uptake (PubMed:3305496, PubMed:7898450,
CC       PubMed:23249124). Probably responsible for energy coupling to the
CC       transport system (Probable). {ECO:0000269|PubMed:23249124,
CC       ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450, ECO:0000305}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ProV),
CC       two transmembrane proteins (ProW) and a solute-binding protein (ProX).
CC       {ECO:0000269|PubMed:23249124}.
CC   -!- INTERACTION:
CC       P14175; P14176: proW; NbExp=2; IntAct=EBI-546797, EBI-8794761;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:16079137}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16079137}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; M24856; AAA24427.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75724.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16542.1; -; Genomic_DNA.
DR   EMBL; X52694; CAA36923.1; -; Genomic_DNA.
DR   PIR; JS0128; BVECPV.
DR   RefSeq; NP_417163.1; NC_000913.3.
DR   RefSeq; WP_000985494.1; NZ_STEB01000042.1.
DR   AlphaFoldDB; P14175; -.
DR   SMR; P14175; -.
DR   BioGRID; 4262264; 24.
DR   BioGRID; 851480; 2.
DR   ComplexPortal; CPX-2126; Glycine/Proline betaine ABC transporter complex.
DR   DIP; DIP-10574N; -.
DR   IntAct; P14175; 6.
DR   STRING; 511145.b2677; -.
DR   TCDB; 3.A.1.12.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P14175; -.
DR   PaxDb; P14175; -.
DR   PRIDE; P14175; -.
DR   EnsemblBacteria; AAC75724; AAC75724; b2677.
DR   EnsemblBacteria; BAA16542; BAA16542; BAA16542.
DR   GeneID; 66673453; -.
DR   GeneID; 947148; -.
DR   KEGG; ecj:JW2652; -.
DR   KEGG; eco:b2677; -.
DR   PATRIC; fig|1411691.4.peg.4064; -.
DR   EchoBASE; EB0764; -.
DR   eggNOG; COG4175; Bacteria.
DR   HOGENOM; CLU_000604_2_2_6; -.
DR   InParanoid; P14175; -.
DR   OMA; GQIFVVM; -.
DR   PhylomeDB; P14175; -.
DR   BioCyc; EcoCyc:PROV-MON; -.
DR   BioCyc; MetaCyc:PROV-MON; -.
DR   PRO; PR:P14175; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISM:EcoCyc.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:1990222; C:ProVWX complex; IPI:ComplexPortal.
DR   GO; GO:0005275; F:amine transmembrane transporter activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR   GO; GO:0005034; F:osmosensor activity; ISM:EcoCyc.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IDA:ComplexPortal.
DR   GO; GO:0031460; P:glycine betaine transport; IDA:ComplexPortal.
DR   GO; GO:1903804; P:glycine import across plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0006972; P:hyperosmotic response; IDA:EcoCyc.
DR   Gene3D; 3.10.580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005892; Gly-betaine_transp_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF00571; CBS; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01186; proV; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Amino-acid transport; ATP-binding; CBS domain; Cell inner membrane;
KW   Cell membrane; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..400
FT                   /note="Glycine betaine/proline betaine transport system
FT                   ATP-binding protein ProV"
FT                   /id="PRO_0000092761"
FT   DOMAIN          29..265
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          282..341
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          343..400
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         61..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   400 AA;  44163 MW;  45A98D45F028B1B9 CRC64;
     MAIKLEIKNL YKIFGEHPQR AFKYIEQGLS KEQILEKTGL SLGVKDASLA IEEGEIFVIM
     GLSGSGKSTM VRLLNRLIEP TRGQVLIDGV DIAKISDAEL REVRRKKIAM VFQSFALMPH
     MTVLDNTAFG MELAGINAEE RREKALDALR QVGLENYAHS YPDELSGGMR QRVGLARALA
     INPDILLMDE AFSALDPLIR TEMQDELVKL QAKHQRTIVF ISHDLDEAMR IGDRIAIMQN
     GEVVQVGTPD EILNNPANDY VRTFFRGVDI SQVFSAKDIA RRTPNGLIRK TPGFGPRSAL
     KLLQDEDREY GYVIERGNKF VGAVSIDSLK TALTQQQGLD AALIDAPLAV DAQTPLSELL
     SHVGQAPCAV PVVDEDQQYV GIISKGMLLR ALDREGVNNG
 
 
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