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YBHS_ECOLI
ID   YBHS_ECOLI              Reviewed;         377 AA.
AC   P0AFQ2; P75775;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable multidrug ABC transporter permease YbhS {ECO:0000305};
GN   Name=ybhS; OrderedLocusNames=b0793, JW0777;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
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   [3]
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   [4]
RP   TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=27112147; DOI=10.1099/mic.0.000292;
RA   Yamanaka Y., Shimada T., Yamamoto K., Ishihama A.;
RT   "Transcription factor CecR (YbiH) regulates a set of genes affecting the
RT   sensitivity of Escherichia coli against cefoperazone and chloramphenicol.";
RL   Microbiology 162:1253-1264(2016).
CC   -!- FUNCTION: Part of the ABC transporter complex YbhFSR that could be
CC       involved in efflux of cefoperazone. Probably involved in the
CC       translocation of the substrate across the membrane.
CC       {ECO:0000305|PubMed:27112147}.
CC   -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC       (YbhF) and two transmembrane proteins (YbhR and YbhS). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Repressed by the transcriptional regulator CecR.
CC       {ECO:0000269|PubMed:27112147}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC73880.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35453.1; -; Genomic_DNA.
DR   PIR; A64816; A64816.
DR   RefSeq; NP_415314.1; NC_000913.3.
DR   RefSeq; WP_000070131.1; NZ_STEB01000019.1.
DR   AlphaFoldDB; P0AFQ2; -.
DR   SMR; P0AFQ2; -.
DR   BioGRID; 4261835; 12.
DR   ComplexPortal; CPX-4443; Sodium/lithium ABC transporter complex.
DR   IntAct; P0AFQ2; 5.
DR   STRING; 511145.b0793; -.
DR   PaxDb; P0AFQ2; -.
DR   PRIDE; P0AFQ2; -.
DR   DNASU; 945411; -.
DR   EnsemblBacteria; AAC73880; AAC73880; b0793.
DR   EnsemblBacteria; BAA35453; BAA35453; BAA35453.
DR   GeneID; 66670935; -.
DR   GeneID; 945411; -.
DR   KEGG; ecj:JW0777; -.
DR   KEGG; eco:b0793; -.
DR   PATRIC; fig|1411691.4.peg.1485; -.
DR   EchoBASE; EB3439; -.
DR   eggNOG; COG0842; Bacteria.
DR   HOGENOM; CLU_039483_8_3_6; -.
DR   InParanoid; P0AFQ2; -.
DR   OMA; STWYLVP; -.
DR   PhylomeDB; P0AFQ2; -.
DR   BioCyc; EcoCyc:YBHS-MON; -.
DR   BioCyc; MetaCyc:YBHS-MON; -.
DR   PRO; PR:P0AFQ2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0090452; P:lithium ion transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0015904; P:tetracycline transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IBA:GO_Central.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; IC:ComplexPortal.
DR   InterPro; IPR000412; ABC_2_transport.
DR   PROSITE; PS51012; ABC_TM2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..377
FT                   /note="Probable multidrug ABC transporter permease YbhS"
FT                   /id="PRO_0000183005"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..261
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..345
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996"
FT   DOMAIN          145..375
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ   SEQUENCE   377 AA;  42060 MW;  C25E40FA4586EEFD CRC64;
     MSNPILSWRR VRALCVKETR QIVRDPSSWL IAVVIPLLLL FIFGYGINLD SSKLRVGILL
     EQRSEAALDF THTMTGSPYI DATISDNRQE LIAKMQAGKI RGLVVIPVDF AEQMERANAT
     APIQVITDGS EPNTANFVQG YVEGIWQIWQ MQRAEDNGQT FEPLIDVQTR YWFNPAAISQ
     HFIIPGAVTI IMTVIGAILT SLVVAREWER GTMEALLSTE ITRTELLLCK LIPYYFLGML
     AMLLCMLVSV FILGVPYRGS LLILFFISSL FLLSTLGMGL LISTITRNQF NAAQVALNAA
     FLPSIMLSGF IFQIDSMPAV IRAVTYIIPA RYFVSTLQSL FLAGNIPVVL VVNVLFLIAS
     AVMFIGLTWL KTKRRLD
 
 
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