KGTP_SHIFL
ID KGTP_SHIFL Reviewed; 432 AA.
AC P0AEX4; P17448;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-ketoglutarate permease;
GN Name=kgtP; OrderedLocusNames=SF2649, S2822;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Uptake of alpha-ketoglutarate across the boundary membrane
CC with the concomitant import of a cation (symport system).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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; AE005674; AAN44145.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17969.1; -; Genomic_DNA.
DR RefSeq; NP_708438.2; NC_004337.2.
DR RefSeq; WP_000841103.1; NZ_WPGW01000044.1.
DR AlphaFoldDB; P0AEX4; -.
DR SMR; P0AEX4; -.
DR STRING; 198214.SF2649; -.
DR PRIDE; P0AEX4; -.
DR EnsemblBacteria; AAN44145; AAN44145; SF2649.
DR EnsemblBacteria; AAP17969; AAP17969; S2822.
DR GeneID; 1026888; -.
DR GeneID; 66673523; -.
DR KEGG; sfl:SF2649; -.
DR KEGG; sfx:S2822; -.
DR PATRIC; fig|198214.7.peg.3159; -.
DR HOGENOM; CLU_001265_39_0_6; -.
DR OMA; THTNDPT; -.
DR OrthoDB; 955823at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000050307"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..62
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..118
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..193
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..279
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..339
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..402
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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
