ID A0A221M9Z8_9BACI Unreviewed; 528 AA.
AC A0A221M9Z8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=L-lactate permease {ECO:0000256|RuleBase:RU365092};
GN ORFNames=CFK40_05295 {ECO:0000313|EMBL:ASN04463.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN04463.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN04463.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN04463.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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; CP022437; ASN04463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221M9Z8; -.
DR KEGG; vne:CFK40_05295; -.
DR OrthoDB; 9761056at2; -.
DR Proteomes; UP000204391; 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 Reference proteome {ECO:0000313|Proteomes:UP000204391};
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 30..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 341..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 380..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 466..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365092"
SQ SEQUENCE 528 AA; 55725 MW; 70B7402088F71A1F CRC64;
MLLFVALCAI IAPFIFLVLL RMTALKGMFF SAIIVIVLAF LIWGMPGTIV IASIFQGTHK
ALTILLILFG AIVLLNTLKH TGAVDRINQG FQNISGDMRV QVVIVAFLFG SLIEGAAGFG
TPAAVTGPLM VALGFNPMAA AVLALVADSS AVSYGAVGTP IQVGLSNVPG ANLALFQEVG
VHIATIDLIA GTFIPFVLVV ILTLFFGKRK GIKDAFTLLP WTLVVGITYT ASALLYAVLF
GHEFVAILGS LTGLVVAAWT AKKGWLMPKT EWNDALQEGF ELETKKSNMG LMTAWSPYVV
VVGLLLITRI IPEVKEFTLT AIDFTWSNIL GVEGITSKWE ILYSPGTILI LAAVLAVIIQ
RKSISNFTKA SKESLLSIKN AGLALLSTLA LVQVFTNSGM NANDFISMPQ YIAQALAGTF
GSMWVFVAPF LGELGAFITG SATVSTLTFS PIQYSIANQT GINTNIVLAL QVIGGAAGNM
ICVHNVVAAS AVVGLSGEEG SIIRKMIIPA LLYGLLAGVG GFILLSFM
//
