GARP_ECO57
ID GARP_ECO57 Reviewed; 444 AA.
AC P0AA81; P42613;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable galactarate/D-glucarate transporter GarP {ECO:0000250|UniProtKB:P0AA80};
DE AltName: Full=D-galactarate permease;
GN Name=garP; OrderedLocusNames=Z4479, ECs4005;
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: Probably involved in the uptake of galactarate and/or D-
CC glucarate (By similarity). May also transport D-glycerate (By
CC similarity). {ECO:0000250|UniProtKB:P0AA80}.
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:0000250|UniProtKB:P0AA80};
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:0000250|UniProtKB:P0AA80};
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:0000250|UniProtKB:P0AA80};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AA80}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58257.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37428.1; -; Genomic_DNA.
DR PIR; E85974; E85974.
DR PIR; E91129; E91129.
DR RefSeq; NP_312032.1; NC_002695.1.
DR RefSeq; WP_000599636.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AA81; -.
DR SMR; P0AA81; -.
DR STRING; 155864.EDL933_4346; -.
DR EnsemblBacteria; AAG58257; AAG58257; Z4479.
DR EnsemblBacteria; BAB37428; BAB37428; ECs_4005.
DR GeneID; 58462947; -.
DR GeneID; 916162; -.
DR KEGG; ece:Z4479; -.
DR KEGG; ecs:ECs_4005; -.
DR PATRIC; fig|386585.9.peg.4179; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR OMA; YNEQSQM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
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_0000121383"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
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
