ID D2TLI5_CITRI Unreviewed; 308 AA.
AC D2TLI5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=High-affinity branched-chain amino acid ABC transporter, permease protein {ECO:0000313|EMBL:CBG91065.1};
GN Name=livH {ECO:0000313|EMBL:CBG91065.1};
GN OrderedLocusNames=ROD_43691 {ECO:0000313|EMBL:CBG91065.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91065.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91065.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91065.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG91065.1; -; Genomic_DNA.
DR RefSeq; WP_012908301.1; NC_013716.1.
DR AlphaFoldDB; D2TLI5; -.
DR STRING; 637910.ROD_43691; -.
DR KEGG; cro:ROD_43691; -.
DR eggNOG; COG0559; Bacteria.
DR HOGENOM; CLU_039929_3_1_6; -.
DR OrthoDB; 9807115at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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; 32960 MW; C3E48968A94687F7 CRC64;
MSEQFLYFLQ QMFNGVTLGS TYALIAIGYT MVYGIIGMIN FAHGEVYMIG SYVSFMIIAA
LMMMGIDTSW LLVAAGFVGA IVIASAYGWS IERVAYRPVR NSKRLIALIS AIGMSIFLQN
YVSLTEGSRD VALPSLFNGQ WVVGASENFS ASITTMQLVI WVVTFIAMLA LTLFIRYSRM
GRACRACAED LKMASLLGIN TDRVIALTFV IGAAMAAVAG VLLGQFYGVI NPYIGFMAGM
KAFTAAVLGG IGSIPGAMIG GLILGVAEAL SSAYLSTEYK DVVSFALLIL VLLVMPTGIL
GRPEVEKV
//
