ID B2TJE5_CLOBB Unreviewed; 514 AA.
AC B2TJE5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=L-lactate permease {ECO:0000256|RuleBase:RU365092};
GN Name=lctP {ECO:0000313|EMBL:ACD22331.1};
GN OrderedLocusNames=CLL_A1363 {ECO:0000313|EMBL:ACD22331.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22331.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Uptake of L-lactate across the membrane. Can also transport
CC D-lactate and glycolate. {ECO:0000256|RuleBase:RU365092}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU365092};
CC Multi-pass membrane protein {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}.
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DR EMBL; CP001056; ACD22331.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TJE5; -.
DR KEGG; cbk:CLL_A1363; -.
DR HOGENOM; CLU_021628_0_0_9; -.
DR Proteomes; UP000001195; 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 membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU365092};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365092};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 104..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 179..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 372..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 397..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 495..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
SQ SEQUENCE 514 AA; 54128 MW; 96E47BF4290BF3C9 CRC64;
MLFLKFLMAI APIIWLIIAL SGLKMPGFKA CLITLVLTMI LAIFFWNLNV IYTMTGVLEG
ILNALWPICL VIVAALFTYN LVLRTGAMDS IKKMLAGVSR DKRVLILIIG WGFGIFMEGM
AGFGTAVAIP ASMLAGLGLN PISAVLACLV ANTAPTAFGS VGIPLVTLSE ITKVGANSLA
ANTAIIEAFI LFISPFIMVC IVGEGIKALK GVFVVTLVAS LSFTIPAYIT ATVLGPELPN
IVGSICCMIC TVASAKIFNK NPQEEYCIQV NEKQEETTLS FSNAVKAWCP FILIFLMLMF
TSTLCPPIHD AIAGFKTSVI VYAGKGGNTL TFSWINTPGV IIFIAAIIGG FTQGAKVPMM
FEVLKGTLKA NWKTIVTICA VMSTAKVMSY SGMISDIASF LVVVTGGAYP LISPLIGSIG
GFVTGSGTST SVLFGGLQVQ TAQKLGLSAA WMGAANTLGA GIGKMICPQS IAIGASAIGK
SGSESKILRS VFKYYICYIT ISGILCFIGT RLFS
//
