KGTP_ECOLI
ID KGTP_ECOLI Reviewed; 432 AA.
AC P0AEX3; P17448;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Alpha-ketoglutarate permease;
GN Name=kgtP; Synonyms=witA; OrderedLocusNames=b2587, JW2571;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2118499; DOI=10.1128/jb.172.9.4745.1990;
RA Seol W., Shatkin A.J.;
RT "A new gene located between pss and rrnG on the Escherichia coli
RT chromosome.";
RL J. Bacteriol. 172:4745-4745(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-183.
RX PubMed=1709493; DOI=10.1093/nar/19.8.1845;
RA Albrechtsen B., Ross B.M., Squires C., Squires C.L.;
RT "Transcriptional termination sequence at the end of the Escherichia coli
RT ribosomal RNA G operon: complex terminators and antitermination.";
RL Nucleic Acids Res. 19:1845-1852(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC STRAIN=K12;
RX PubMed=2190187; DOI=10.1093/nar/18.10.3056;
RA Seol W., Shatkin A.J.;
RT "Sequence of the distal end of E. coli ribosomal RNA rrnG operon.";
RL Nucleic Acids Res. 18:3056-3056(1990).
RN [7]
RP FUNCTION.
RX PubMed=2053984; DOI=10.1073/pnas.88.9.3802;
RA Seol W., Shatkin A.J.;
RT "Escherichia coli kgtP encodes an alpha-ketoglutarate transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3802-3806(1991).
RN [8]
RP TOPOLOGY.
RX PubMed=8419306; DOI=10.1128/jb.175.2.565-567.1993;
RA Seol W., Shatkin A.J.;
RT "Membrane topology model of Escherichia coli alpha-ketoglutarate permease
RT by phoA fusion analysis.";
RL J. Bacteriol. 175:565-567(1993).
RN [9]
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 alpha-ketoglutarate across the boundary membrane
CC with the concomitant import of a cation (symport system).
CC {ECO:0000269|PubMed:2053984}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Metabolite:H+
CC Symporter (MHS) family (TC 2.A.1.6) family. {ECO:0000305}.
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DR EMBL; X53027; CAA37198.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75640.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16472.1; -; Genomic_DNA.
DR EMBL; X56780; CAA40099.1; ALT_TERM; Genomic_DNA.
DR EMBL; X52363; CAA36589.1; -; Genomic_DNA.
DR PIR; JN0080; JN0080.
DR RefSeq; NP_417082.1; NC_000913.3.
DR RefSeq; WP_000841103.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0AEX3; -.
DR SMR; P0AEX3; -.
DR BioGRID; 4260613; 10.
DR STRING; 511145.b2587; -.
DR TCDB; 2.A.1.6.2; the major facilitator superfamily (mfs).
DR jPOST; P0AEX3; -.
DR PaxDb; P0AEX3; -.
DR PRIDE; P0AEX3; -.
DR EnsemblBacteria; AAC75640; AAC75640; b2587.
DR EnsemblBacteria; BAA16472; BAA16472; BAA16472.
DR GeneID; 66673523; -.
DR GeneID; 947069; -.
DR KEGG; ecj:JW2571; -.
DR KEGG; eco:b2587; -.
DR PATRIC; fig|1411691.4.peg.4147; -.
DR EchoBASE; EB0517; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_39_0_6; -.
DR InParanoid; P0AEX3; -.
DR OMA; THTNDPT; -.
DR PhylomeDB; P0AEX3; -.
DR BioCyc; EcoCyc:KGTP-MON; -.
DR BioCyc; MetaCyc:KGTP-MON; -.
DR PRO; PR:P0AEX3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015294; F:solute:cation symporter activity; IDA:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004736; MHS_symport.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00883; 2A0106; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 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..432
FT /note="Alpha-ketoglutarate permease"
FT /id="PRO_0000050306"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 54..62
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 84..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 96..116
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 117..118
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 119..139
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 184..193
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 194..214
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 215..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 244..264
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 265..279
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 280..300
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TOPO_DOM 301..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 310..330
FT /note="Helical; Name=9"
FT /evidence="ECO:0000305"
FT TOPO_DOM 331..339
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 340..360
FT /note="Helical; Name=10"
FT /evidence="ECO:0000305"
FT TOPO_DOM 361..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 374..394
FT /note="Helical; Name=11"
FT /evidence="ECO:0000305"
FT TOPO_DOM 395..402
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
FT TRANSMEM 403..423
FT /note="Helical; Name=12"
FT /evidence="ECO:0000305"
FT TOPO_DOM 424..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8419306"
SQ SEQUENCE 432 AA; 47052 MW; 264B8473195765DB CRC64;
MAESTVTADS KLTSSDTRRR IWAIVGASSG NLVEWFDFYV YSFCSLYFAH IFFPSGNTTT
QLLQTAGVFA AGFLMRPIGG WLFGRIADKH GRKKSMLLSV CMMCFGSLVI ACLPGYETIG
TWAPALLLLA RLFQGLSVGG EYGTSATYMS EVAVEGRKGF YASFQYVTLI GGQLLALLVV
VVLQHTMEDA ALREWGWRIP FALGAVLAVV ALWLRRQLDE TSQQETRALK EAGSLKGLWR
NRRAFIMVLG FTAAGSLCFY TFTTYMQKYL VNTAGMHANV ASGIMTAALF VFMLIQPLIG
ALSDKIGRRT SMLCFGSLAA IFTVPILSAL QNVSSPYAAF GLVMCALLIV SFYTSISGIL
KAEMFPAQVR ALGVGLSYAV ANAIFGGSAE YVALSLKSIG METAFFWYVT LMAVVAFLVS
LMLHRKGKGM RL
