LIVH_ECOLI
ID LIVH_ECOLI Reviewed; 308 AA.
AC P0AEX7; P08340; Q2M7C0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=High-affinity branched-chain amino acid transport system permease protein LivH;
DE AltName: Full=LIV-I protein H;
GN Name=livH; OrderedLocusNames=b3457, JW3422;
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=3009409; DOI=10.1128/jb.166.2.565-573.1986;
RA Nazos P.M., Antonucci T.K., Landick R., Oxender D.L.;
RT "Cloning and characterization of livH, the structural gene encoding a
RT component of the leucine transport system in Escherichia coli.";
RL J. Bacteriol. 166:565-573(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2195019; DOI=10.1016/s0021-9258(19)38417-0;
RA Adams M.D., Wagner L.M., Graddis T.J., Landick R., Antonucci T.K.,
RA Gibson A.L., Oxender D.L.;
RT "Nucleotide sequence and genetic characterization reveal six essential
RT genes for the LIV-I and LS transport systems of Escherichia coli.";
RL J. Biol. Chem. 265:11436-11443(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 TOPOLOGY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC branched-chain amino acids. Probably responsible for the translocation
CC of the substrates across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. LivHM subfamily. {ECO:0000305}.
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DR EMBL; J05516; AAA83884.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18432.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76482.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77836.1; -; Genomic_DNA.
DR PIR; S47676; QRECLH.
DR RefSeq; NP_417914.1; NC_000913.3.
DR RefSeq; WP_001295111.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P0AEX7; -.
DR BioGRID; 4262494; 24.
DR ComplexPortal; CPX-4316; Branched chain amino acid ABC transporter complex.
DR ComplexPortal; CPX-4317; Branched chain amino acid, leucine-specific ABC transporter complex.
DR STRING; 511145.b3457; -.
DR TCDB; 3.A.1.4.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AEX7; -.
DR PRIDE; P0AEX7; -.
DR EnsemblBacteria; AAC76482; AAC76482; b3457.
DR EnsemblBacteria; BAE77836; BAE77836; BAE77836.
DR GeneID; 67417084; -.
DR GeneID; 947965; -.
DR KEGG; ecj:JW3422; -.
DR KEGG; eco:b3457; -.
DR PATRIC; fig|1411691.4.peg.3269; -.
DR EchoBASE; EB0533; -.
DR eggNOG; COG0559; Bacteria.
DR HOGENOM; CLU_039929_3_1_6; -.
DR InParanoid; P0AEX7; -.
DR OMA; NMGWFLI; -.
DR PhylomeDB; P0AEX7; -.
DR BioCyc; EcoCyc:LIVH-MON; -.
DR BioCyc; MetaCyc:LIVH-MON; -.
DR PRO; PR:P0AEX7; -.
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:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005304; F:L-valine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015803; P:branched-chain amino acid transport; IMP:EcoCyc.
DR GO; GO:0042941; P:D-alanine transport; IBA:GO_Central.
DR GO; GO:1903714; P:isoleucine transmembrane transport; IMP:EcoCyc.
DR GO; GO:0015808; P:L-alanine transport; IBA:GO_Central.
DR GO; GO:1903806; P:L-isoleucine import across plasma membrane; IBA:GO_Central.
DR GO; GO:1903785; P:L-valine transmembrane transport; IMP:EcoCyc.
DR GO; GO:0098713; P:leucine import across plasma membrane; IMP:EcoCyc.
DR GO; GO:0015823; P:phenylalanine transport; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001851; ABC_transp_permease.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..308
FT /note="High-affinity branched-chain amino acid transport
FT system permease protein LivH"
FT /id="PRO_0000060058"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..45
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..203
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..280
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 253
FT /note="S -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 32982 MW; 8C8A4BD56718A4BE CRC64;
MSEQFLYFLQ QMFNGVTLGS TYALIAIGYT MVYGIIGMIN FAHGEVYMIG SYVSFMIIAA
LMMMGIDTGW LLVAAGFVGA IVIASAYGWS IERVAYRPVR NSKRLIALIS AIGMSIFLQN
YVSLTEGSRD VALPSLFNGQ WVVGHSENFS ASITTMQAVI WIVTFLAMLA LTIFIRYSRM
GRACRACAED LKMASLLGIN TDRVIALTFV IGAAMAAVAG VLLGQFYGVI NPYIGFMAGM
KAFTAAVLGG IGSIPGAMIG GLILGIAEAL SSAYLSTEYK DVVSFALLIL VLLVMPTGIL
GRPEVEKV
