ID D3VC52_XENNA Unreviewed; 526 AA.
AC D3VC52;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=L-lactate permease {ECO:0000256|RuleBase:RU365092};
GN OrderedLocusNames=XNC1_1643 {ECO:0000313|EMBL:CBJ89705.1};
OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS 1036 / NCIMB 9965 / AN6).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ89705.1, ECO:0000313|Proteomes:UP000008075};
RN [1] {ECO:0000313|EMBL:CBJ89705.1, ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 /
RC AN6 {ECO:0000313|Proteomes:UP000008075};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
CC -!- FUNCTION: Uptake of L-lactate across the membrane. Can also transport
CC D-lactate and glycolate. {ECO:0000256|RuleBase:RU365092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate(in) + H(+)(in) = (R)-lactate(out) + H(+)(out);
CC Xref=Rhea:RHEA:71791, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004;
CC Evidence={ECO:0000256|ARBA:ARBA00034057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71793;
CC Evidence={ECO:0000256|ARBA:ARBA00034057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651;
CC Evidence={ECO:0000256|ARBA:ARBA00034011};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417;
CC Evidence={ECO:0000256|ARBA:ARBA00034011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate(in) + H(+)(in) = glycolate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29411, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805;
CC Evidence={ECO:0000256|ARBA:ARBA00034062};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29413;
CC Evidence={ECO:0000256|ARBA:ARBA00034062};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365092}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU365092}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the lactate permease family.
CC {ECO:0000256|ARBA:ARBA00010100, ECO:0000256|RuleBase:RU365092}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365092}.
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DR EMBL; FN667742; CBJ89705.1; -; Genomic_DNA.
DR RefSeq; WP_010847237.1; NC_014228.1.
DR AlphaFoldDB; D3VC52; -.
DR STRING; 406817.XNC1_1643; -.
DR KEGG; xne:XNC1_1643; -.
DR eggNOG; COG1620; Bacteria.
DR HOGENOM; CLU_021628_4_1_6; -.
DR Proteomes; UP000008075; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR003804; Lactate_perm.
DR NCBIfam; TIGR00795; lctP; 1.
DR PANTHER; PTHR30003:SF0; GLYCOLATE PERMEASE GLCA; 1.
DR PANTHER; PTHR30003; L-LACTATE PERMEASE; 1.
DR Pfam; PF02652; Lactate_perm; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|RuleBase:RU365092};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365092};
KW Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365092};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365092};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365092}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 49..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 308..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 343..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 387..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 415..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 507..525
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
SQ SEQUENCE 526 AA; 56741 MW; C60974D9CFD7E9D7 CRC64;
MPLFFSIAPI ALLIWMMTKH NGIPSFIALP LTAVMVYLIQ AFWFGVQPIL LYANIIAAWI
SVFTPITIIL GAILLHKLMQ ISGAEEVVRH WLGNISSNLV AQLMIIGWAF AFMIEGASGF
GTPAAIAAPI LVGLGFNPLR VVLLTLVMNS VPVSFGAVGT PTWFGFANLG LPDDNLLEIG
RLSACIHFVA GFIIPLLALR FIVSWQEIRQ NIFFIFLSIL SCTVPYLLLA QINYEFPALM
GGAIGLVLSV LLARMGVGIK RYEKRDPGQV VPVSKIVKAM APIMLLITIL VITRIHQLGI
KALLNNAAII WQVSLGWLGD LSVSQSLIIS FQQLLGTSAS ASYKVLYVPA IIPFLLVVLV
CMALFQLNLH QVKQIFCETG SRIFKPFIAL FGALVMVNMM MLGDENSPVF IIGKALAAMT
GEGWLLFSSF MGALGAFFSG SNTVSNLTFG GIQHSIALNN GMNVNLVLAL QSVGGAMGNM
ICLNNIIAVC SILGISNAEG QIMKKTILPM LVYWGIAAVM ALILAS
//
