LLDP_ECOLI
ID LLDP_ECOLI Reviewed; 551 AA.
AC P33231; Q2M7R7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=L-lactate permease {ECO:0000305};
GN Name=lldP {ECO:0000303|PubMed:11283302};
GN Synonyms=lctP {ECO:0000303|PubMed:8407843};
GN OrderedLocusNames=b3603, JW3578;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=8407843; DOI=10.1128/jb.175.20.6671-6678.1993;
RA Dong J.M., Taylor J.S., Latour D.J., Iuchi S., Lin E.C.C.;
RT "Three overlapping lct genes involved in L-lactate utilization by
RT Escherichia coli.";
RL J. Bacteriol. 175:6671-6678(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11283302; DOI=10.1099/00221287-147-4-1069;
RA Nunez M.F., Pellicer M.T., Badia J., Aguilar J., Baldoma L.;
RT "The gene yghK linked to the glc operon of Escherichia coli encodes a
RT permease for glycolate that is structurally and functionally similar to L-
RT lactate permease.";
RL Microbiology 147:1069-1077(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11785976; DOI=10.1006/bbrc.2001.6255;
RA Nunez M.F., Kwon O., Wilson T.H., Aguilar J., Baldoma L., Lin E.C.C.;
RT "Transport of L-lactate, D-lactate, and glycolate by the LldP and GlcA
RT membrane carriers of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 290:824-829(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Uptake of L-lactate across the membrane (PubMed:11283302,
CC PubMed:11785976). Can also transport D-lactate and glycolate
CC (PubMed:11283302, PubMed:11785976). Seems to be driven by a proton
CC motive force (PubMed:11785976). {ECO:0000269|PubMed:11283302,
CC ECO:0000269|PubMed:11785976}.
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:0000269|PubMed:11785976};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417;
CC Evidence={ECO:0000269|PubMed:11785976};
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:0000269|PubMed:11785976};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71793;
CC Evidence={ECO:0000269|PubMed:11785976};
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:0000269|PubMed:11785976};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29413;
CC Evidence={ECO:0000269|PubMed:11785976};
CC -!- ACTIVITY REGULATION: Inhibited by the proton ionophore carbonyl cyanide
CC m-chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:11785976}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By L-lactate; aerobically. {ECO:0000269|PubMed:8407843}.
CC -!- DISRUPTION PHENOTYPE: The glcA-lldP double mutant is unable to grow on
CC glycolate and displays undetectable glycolate uptake when grown in the
CC presence of glycolate. {ECO:0000269|PubMed:11283302}.
CC -!- SIMILARITY: Belongs to the lactate permease family. {ECO:0000305}.
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DR EMBL; L13970; AAA03583.1; -; Unassigned_DNA.
DR EMBL; U00039; AAB18580.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76627.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77689.1; -; Genomic_DNA.
DR PIR; A49904; A49904.
DR RefSeq; NP_418060.1; NC_000913.3.
DR RefSeq; WP_001295233.1; NZ_SSZK01000022.1.
DR AlphaFoldDB; P33231; -.
DR BioGRID; 4261271; 6.
DR DIP; DIP-10109N; -.
DR IntAct; P33231; 1.
DR STRING; 511145.b3603; -.
DR TCDB; 2.A.14.1.1; the lactate permease (lctp) family.
DR jPOST; P33231; -.
DR PaxDb; P33231; -.
DR PRIDE; P33231; -.
DR EnsemblBacteria; AAC76627; AAC76627; b3603.
DR EnsemblBacteria; BAE77689; BAE77689; BAE77689.
DR GeneID; 948114; -.
DR KEGG; ecj:JW3578; -.
DR KEGG; eco:b3603; -.
DR PATRIC; fig|1411691.4.peg.3103; -.
DR EchoBASE; EB1904; -.
DR eggNOG; COG1620; Bacteria.
DR HOGENOM; CLU_021628_0_0_6; -.
DR InParanoid; P33231; -.
DR OMA; LFVYKMP; -.
DR PhylomeDB; P33231; -.
DR BioCyc; EcoCyc:LCTP-MON; -.
DR BioCyc; MetaCyc:LCTP-MON; -.
DR PRO; PR:P33231; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR InterPro; IPR003804; Lactate_perm.
DR PANTHER; PTHR30003; PTHR30003; 1.
DR Pfam; PF02652; Lactate_perm; 1.
DR TIGRFAMs; TIGR00795; lctP; 1.
PE 1: Evidence at protein level;
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_0000210374"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
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 220..240
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; 59168 MW; 086DFDB410E2027B 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 FTCIVGVITT
LQAYVLTWMI P
