GLCA_ECOLI
ID GLCA_ECOLI Reviewed; 560 AA.
AC Q46839; Q2M9M1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glycolate permease GlcA;
GN Name=glcA {ECO:0000303|PubMed:11283302}; Synonyms=yghK;
GN OrderedLocusNames=b2975, JW2942;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, INDUCTION, 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 [4]
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 [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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 glycolate across the membrane (PubMed:11283302,
CC PubMed:11785976). Can also transport L-lactate and D-lactate
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=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 -!- 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 -!- 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 glycolate. {ECO:0000269|PubMed:11283302}.
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; U28377; AAA69142.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76011.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77035.1; -; Genomic_DNA.
DR PIR; E65083; E65083.
DR RefSeq; NP_417449.1; NC_000913.3.
DR RefSeq; WP_000259302.1; NZ_SSUV01000003.1.
DR AlphaFoldDB; Q46839; -.
DR BioGRID; 851589; 1.
DR DIP; DIP-12206N; -.
DR IntAct; Q46839; 2.
DR STRING; 511145.b2975; -.
DR TCDB; 2.A.14.1.2; the lactate permease (lctp) family.
DR PaxDb; Q46839; -.
DR PRIDE; Q46839; -.
DR EnsemblBacteria; AAC76011; AAC76011; b2975.
DR EnsemblBacteria; BAE77035; BAE77035; BAE77035.
DR GeneID; 947259; -.
DR KEGG; ecj:JW2942; -.
DR KEGG; eco:b2975; -.
DR PATRIC; fig|1411691.4.peg.3756; -.
DR EchoBASE; EB2818; -.
DR eggNOG; COG1620; Bacteria.
DR HOGENOM; CLU_021628_0_0_6; -.
DR InParanoid; Q46839; -.
DR OMA; VIVLWIQ; -.
DR PhylomeDB; Q46839; -.
DR BioCyc; EcoCyc:B2975-MON; -.
DR BioCyc; MetaCyc:B2975-MON; -.
DR PRO; PR:Q46839; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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 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..560
FT /note="Glycolate permease GlcA"
FT /id="PRO_0000210380"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..41
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..130
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..199
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..248
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..378
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..438
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..560
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 560 AA; 58920 MW; 8ECB9F9626FFC40A CRC64;
MVTWTQMYMP MGGLGLSALV ALIPIIFFFV ALAVLRLKGH VAGAITLILS ILIAIFAFKM
PIDMAFAAAG YGFIYGLWPI AWIIVAAVFL YKLTVASGQF DIIRSSVISI TDDQRLQVLL
IGFSFGALLE GAAGFGAPVA ITGALLVGLG FKPLYAAGLC LIANTAPVAF GALGVPILVA
GQVTGIDPFH IGAMAGRQLP FLSVLVPFWL VAMMDGWKGV KETWPAALVA GGSFAVTQFF
TSNYIGPELP DITSALVSIV SLALFLKVWR PKNTETAISM GQSAGAMVVN KPSSGGPVPS
EYSLGQIIRA WSPFLILTVL VTIWTMKPFK ALFAPGGAFY SLVINFQIPH LHQQVLKAAP
IVAQPTPMDA VFKFDPLSAG GTAIFIAAII SIFILGVGIK KGIGVFAETL ISLKWPILSI
GMVLAFAFVT NYSGMSTTLA LVLAGTGVMF PFFSPFLGWL GVFLTGSDTS SNALFGSLQS
TTAQQINVSD TLLVAANTSG GVTGKMISPQ SIAVACAATG MVGRESELFR YTVKHSLIFA
SVIGIITLLQ AYVFTGMLVS
