YBHR_ECOLI
ID YBHR_ECOLI Reviewed; 368 AA.
AC P0AFP9; P75774; Q9ZBC6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable multidrug ABC transporter permease YbhR {ECO:0000305};
GN Name=ybhR; OrderedLocusNames=b0792, JW5803;
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], AND SEQUENCE REVISION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC73879.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35451.2; -; Genomic_DNA.
DR PIR; H64815; H64815.
DR RefSeq; NP_415313.1; NC_000913.3.
DR RefSeq; WP_000469031.1; NZ_STEB01000019.1.
DR AlphaFoldDB; P0AFP9; -.
DR SMR; P0AFP9; -.
DR BioGRID; 4261834; 20.
DR ComplexPortal; CPX-4443; Sodium/lithium ABC transporter complex.
DR DIP; DIP-48088N; -.
DR IntAct; P0AFP9; 1.
DR STRING; 511145.b0792; -.
DR TCDB; 3.A.1.105.15; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AFP9; -.
DR PaxDb; P0AFP9; -.
DR PRIDE; P0AFP9; -.
DR DNASU; 945403; -.
DR EnsemblBacteria; AAC73879; AAC73879; b0792.
DR EnsemblBacteria; BAA35451; BAA35451; BAA35451.
DR GeneID; 66670936; -.
DR GeneID; 945403; -.
DR KEGG; ecj:JW5803; -.
DR KEGG; eco:b0792; -.
DR PATRIC; fig|1411691.4.peg.1486; -.
DR EchoBASE; EB3438; -.
DR eggNOG; COG0842; Bacteria.
DR HOGENOM; CLU_039483_8_3_6; -.
DR InParanoid; P0AFP9; -.
DR OMA; WGQELIE; -.
DR PhylomeDB; P0AFP9; -.
DR BioCyc; EcoCyc:YBHR-MON; -.
DR BioCyc; MetaCyc:YBHR-MON; -.
DR PRO; PR:P0AFP9; -.
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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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 PRINTS; PR00164; ABC2TRNSPORT.
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..368
FT /note="Probable multidrug ABC transporter permease YbhR"
FT /id="PRO_0000183002"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..173
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..253
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..339
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 129..366
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ SEQUENCE 368 AA; 41566 MW; CD9380B094EB86F2 CRC64;
MFHRLWTLIR KELQSLLREP QTRAILILPV LIQVILFPFA ATLEVTNATI AIYDEDNGEH
SVELTQRFAR ASAFTHVLLL KSPQEIRPTI DTQKALLLVR FPADFSRKLD TFQTAPLQLI
LDGRNSNSAQ IAANYLQQIV KNYQQELLEG KPKPNNSELV VRNWYNPNLD YKWFVVPSLI
AMITTIGVMI VTSLSVARER EQGTLDQLLV SPLTTWQIFI GKAVPALIVA TFQATIVLAI
GIWAYQIPFA GSLALFYFTM VIYGLSLVGF GLLISSLCST QQQAFIGVFV FMMPAILLSG
YVSPVENMPV WLQNLTWINP IRHFTDITKQ IYLKDASLDI VWNSLWPLLV ITATTGSAAY
AMFRRKVM
