ID A7GL71_BACCN Unreviewed; 539 AA.
AC A7GL71;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=L-lactate permease {ECO:0000256|RuleBase:RU365092};
GN OrderedLocusNames=Bcer98_0527 {ECO:0000313|EMBL:ABS20879.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20879.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS20879.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS20879.1; -; Genomic_DNA.
DR RefSeq; WP_011983635.1; NC_009674.1.
DR AlphaFoldDB; A7GL71; -.
DR STRING; 315749.Bcer98_0527; -.
DR GeneID; 56416095; -.
DR KEGG; bcy:Bcer98_0527; -.
DR eggNOG; COG1620; Bacteria.
DR HOGENOM; CLU_021628_0_0_9; -.
DR OrthoDB; 9761056at2; -.
DR Proteomes; UP000002300; 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 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 64..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 436..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 519..538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
SQ SEQUENCE 539 AA; 57620 MW; 0C330222F93865B8 CRC64;
MNTWTQIYDP LNNIWLSALI AALPIFCFII CLTGFKMKGY ISGLYSVIVA VIIAIFVYKM
PTTAAVASAG FGILSGFYPI CTIVIAAIFL YKITVKTEQF NVIRDSISSI TSDQRLQVLL
IAYSFGAFLE GAAGFGVPVA ITAALLVGMG FNPLKAAGIC LVANIAGGAM GAMGIPVTVP
AQLTQLDALT VGRHTVTILP FISIILPFLL VAMVDGFKGI KETWQGILVS GVSFAITQFT
VTYFLGAELT DIFAAVVSMV ALTLFLRVWQ PKSSAKEEKQ EEKQSHTFNQ ILYAWSPFVF
LTAFVTIFNL KPIKALFAPK GALESLVFNI QFPGLHNQVI KTAPITKADT PFAGIFKLDV
FSSTTTAIVL AIIVSLILYR VNGKMIKELI IETLKELKAP VYTICSVIAL AYVENYSGMS
STLGLAFSST GNVFPILSPI LGWIGVFITG SVVSSGSLFA PLQAVTAAQL DIVPSTLVAL
NVVGGTMAKM VSPQSVAVAC AAVGLVGKES ALFKVAMKYS LIFLAIISLL QLNSIFHIF
//
