LLDP_ECO57
ID LLDP_ECO57 Reviewed; 551 AA.
AC P65254; Q8XDF9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=L-lactate permease {ECO:0000250|UniProtKB:P33231};
GN Name=lldP; Synonyms=lctP; OrderedLocusNames=Z5030, ECs4481;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Uptake of L-lactate across the membrane (By similarity). Can
CC also transport D-lactate and glycolate (By similarity). Seems to be
CC driven by a proton motive force (By similarity).
CC {ECO:0000250|UniProtKB:P33231}.
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:0000250|UniProtKB:P33231};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417;
CC Evidence={ECO:0000250|UniProtKB:P33231};
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:0000250|UniProtKB:P33231};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71793;
CC Evidence={ECO:0000250|UniProtKB:P33231};
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:0000250|UniProtKB:P33231};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29413;
CC Evidence={ECO:0000250|UniProtKB:P33231};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P33231}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the lactate permease family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58750.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37904.1; -; Genomic_DNA.
DR PIR; A98189; A98189.
DR PIR; B86036; B86036.
DR RefSeq; NP_312508.1; NC_002695.1.
DR RefSeq; WP_001297977.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P65254; -.
DR STRING; 155864.EDL933_4867; -.
DR EnsemblBacteria; AAG58750; AAG58750; Z5030.
DR EnsemblBacteria; BAB37904; BAB37904; ECs_4481.
DR GeneID; 66672499; -.
DR GeneID; 915577; -.
DR KEGG; ece:Z5030; -.
DR KEGG; ecs:ECs_4481; -.
DR PATRIC; fig|386585.9.peg.4696; -.
DR eggNOG; COG1620; Bacteria.
DR HOGENOM; CLU_021628_0_0_6; -.
DR OMA; LFVYKMP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR003804; Lactate_perm.
DR PANTHER; PTHR30003; PTHR30003; 1.
DR Pfam; PF02652; Lactate_perm; 1.
DR TIGRFAMs; TIGR00795; lctP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..551
FT /note="L-lactate permease"
FT /id="PRO_0000210376"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 59186 MW; 086A907410E2027B CRC64;
MNLWQQNYDP AGNIWLSSLI ASLPILFFFF ALIKLKLKGY VAASWTVAIA LAVALLFYKM
PVANALASVV YGFFYGLWPI AWIIIAAVFV YKISVKTGQF DIIRSSILSI TPDQRLQMLI
VGFCFGAFLE GAAGFGAPVA ITAALLVGLG FKPLYAAGLC LIVNTAPVAF GAMGIPILVA
GQVTGIDSFE IGQMVGRQLP FMTIIVLFWI MAIMDGWRGI KETWPAVVVA GGSFAIAQYL
SSNFIGPELP DIISSLVSLL CLTLFLKRWQ PVRVFRFGDL GASQVDMTLA HTGYTAGQVL
RAWTPFLFLT ATVTLWSIPP FKALFASGGA LYEWVINIPV PYLDKLVARM PPVVSEATAY
AAVFKFDWFS ATGTAILFAA LLSIVWLKMK PSDAISTFGS TLKELALPIY SIGMVLAFAF
ISNYSGLSST LALALAHTGH AFTFFSPFLG WLGVFLTGSD TSSNALFAAL QATAAQQIGV
SDLLLVAANT TGGVTGKMIS PQSIAIACAA VGLVGKESDL FRFTVKHSLI FTCMVGVITT
LQAYVLTWMI P
