ID GARP_ECOLI Reviewed; 444 AA.
AC P0AA80; P42613; Q2M982;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Probable galactarate/D-glucarate transporter GarP {ECO:0000305};
GN Name=garP {ECO:0000303|PubMed:10762278}; Synonyms=yhaU;
GN OrderedLocusNames=b3127, JW3096;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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 POSSIBLE FUNCTION.
RX PubMed=9772162; DOI=10.1021/bi981124f;
RA Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily:
RT characterization of the (D)-glucarate/galactarate catabolic pathway in
RT Escherichia coli.";
RL Biochemistry 37:14369-14375(1998).
RN [4]
RP POSSIBLE FUNCTION, INDUCTION, AND GENE NAME.
RX PubMed=10762278; DOI=10.1128/jb.182.9.2672-2674.2000;
RA Monterrubio R., Baldoma L., Obradors N., Aguilar J., Badia J.;
RT "A common regulator for the operons encoding the enzymes involved in D-
RT galactarate, D-glucarate, and D-glycerate utilization in Escherichia
RT coli.";
RL J. Bacteriol. 182:2672-2674(2000).
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: Probably involved in the uptake of galactarate and/or D-
CC glucarate (Probable). May also transport D-glycerate (Probable).
CC {ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactarate(in) + H(+)(in) = galactarate(out) + H(+)(out);
CC Xref=Rhea:RHEA:28478, ChEBI:CHEBI:15378, ChEBI:CHEBI:16537;
CC Evidence={ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucarate(in) + H(+)(in) = D-glucarate(out) + H(+)(out);
CC Xref=Rhea:RHEA:28474, ChEBI:CHEBI:15378, ChEBI:CHEBI:30612;
CC Evidence={ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate(in) + H(+)(in) = (R)-glycerate(out) + H(+)(out);
CC Xref=Rhea:RHEA:70927, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659;
CC Evidence={ECO:0000305|PubMed:10762278};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced in the presence of D-galactarate, D-glucarate or D-
CC glycerate. {ECO:0000269|PubMed:10762278}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
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DR EMBL; U18997; AAA57930.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76161.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77174.1; -; Genomic_DNA.
DR PIR; C65102; C65102.
DR RefSeq; NP_417596.1; NC_000913.3.
DR RefSeq; WP_000599636.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AA80; -.
DR SMR; P0AA80; -.
DR BioGRID; 4259486; 14.
DR STRING; 511145.b3127; -.
DR jPOST; P0AA80; -.
DR PaxDb; 511145-b3127; -.
DR EnsemblBacteria; AAC76161; AAC76161; b3127.
DR GeneID; 75203757; -.
DR GeneID; 947642; -.
DR KEGG; ecj:JW3096; -.
DR KEGG; eco:b3127; -.
DR PATRIC; fig|1411691.4.peg.3605; -.
DR EchoBASE; EB2613; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR InParanoid; P0AA80; -.
DR OMA; YNEQSQM; -.
DR OrthoDB; 9771451at2; -.
DR PhylomeDB; P0AA80; -.
DR BioCyc; EcoCyc:YHAU-MONOMER; -.
DR BioCyc; MetaCyc:YHAU-MONOMER; -.
DR PRO; PR:P0AA80; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; ISM:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042836; P:D-glucarate metabolic process; IMP:EcoCyc.
DR GO; GO:0019580; P:galactarate metabolic process; IEP:EcoCyc.
DR GO; GO:0098656; P:monoatomic anion transmembrane transport; IEA:GOC.
DR CDD; cd17319; MFS_ExuT_GudP_like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000849; Sugar_P_transporter.
DR NCBIfam; TIGR00893; 2A0114; 1.
DR PANTHER; PTHR11662:SF399; GH23975P; 1.
DR PANTHER; PTHR11662; SOLUTE CARRIER FAMILY 17; 1.
DR Pfam; PF07690; MFS_1; 2.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..444
FT /note="Probable galactarate/D-glucarate transporter GarP"
FT /id="PRO_0000121382"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..56
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..288
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..350
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..413
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 444 AA; 49009 MW; 48FA27023B0C9D30 CRC64;
MILDTVDEKK KGVHTRYLIL LIIFIVTAVN YADRATLSIA GTEVAKELQL SAVSMGYIFS
AFGWAYLLMQ IPGGWLLDKF GSKKVYTYSL FFWSLFTFLQ GFVDMFPLAW AGISMFFMRF
MLGFSEAPSF PANARIVAAW FPTKERGTAS AIFNSAQYFS LALFSPLLGW LTFAWGWEHV
FTVMGVIGFV LTALWIKLIH NPTDHPRMSA EELKFISENG AVVDMDHKKP GSAAASGPKL
HYIKQLLSNR MMLGVFFGQY FINTITWFFL TWFPIYLVQE KGMSILKVGL VASIPALCGF
AGGVLGGVFS DYLIKRGLSL TLARKLPIVL GMLLASTIIL CNYTNNTTLV VMLMALAFFG
KGFGALGWPV ISDTAPKEIV GLCGGVFNVF GNVASIVTPL VIGYLVSELH SFNAALVFVG
CSALMAMVCY LFVVGDIKRM ELQK
//
