ID Q1R5H1_ECOUT Unreviewed; 308 AA.
AC Q1R5H1;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=High-affinity branched-chain amino acid transport system permease protein livH {ECO:0000313|EMBL:ABE09393.1};
GN Name=livH {ECO:0000313|EMBL:ABE09393.1};
GN OrderedLocusNames=UTI89_C3964 {ECO:0000313|EMBL:ABE09393.1};
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09393.1, ECO:0000313|Proteomes:UP000001952};
RN [1] {ECO:0000313|EMBL:ABE09393.1, ECO:0000313|Proteomes:UP000001952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. LivHM subfamily. {ECO:0000256|ARBA:ARBA00037998}.
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DR EMBL; CP000243; ABE09393.1; -; Genomic_DNA.
DR RefSeq; WP_001295101.1; NZ_CP064825.1.
DR AlphaFoldDB; Q1R5H1; -.
DR KEGG; eci:UTI89_C3964; -.
DR HOGENOM; CLU_039929_3_1_6; -.
DR OMA; NMGWFLI; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd06582; TM_PBP1_LivH_like; 1.
DR InterPro; IPR001851; ABC_transp_permease.
DR PANTHER; PTHR11795; BRANCHED-CHAIN AMINO ACID TRANSPORT SYSTEM PERMEASE PROTEIN LIVH; 1.
DR PANTHER; PTHR11795:SF371; HIGH-AFFINITY BRANCHED-CHAIN AMINO ACID TRANSPORT SYSTEM PERMEASE PROTEIN LIVH; 1.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 3: Inferred from homology;
KW Amino-acid transport {ECO:0000256|ARBA:ARBA00022970};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 308 AA; 32992 MW; 3757F9BF31CAD80C CRC64;
MSEQFLYFLQ QMFNGVTLGS TYALIAIGYT MVYGIIGMIN FAHGEVYMIG SYVSFMIIAA
LMMLGIDTGW LLVVAGFVGA IVIASAYGWS IERVAYRPVR NSKRLIALIS AIGMSIFLQN
YVSLTEGSRD VALPSLFNGQ WVVGHSENFS ASITTMQAVI WIVTFLAMLA LTIFIRYSRM
GRACRACAED LKMASLLGIN TDRVIALTFV IGAAMAAVAG VLLGQFYGVI NPYIGFMAGM
KAFTAAVLGG IGSIPGAMIG GLILGIAEAL SSAYLSTEYK DVVSFALLIL VLLVMPTGIL
GRPEVEKV
//