CITA_SALTI
ID CITA_SALTI Reviewed; 434 AA.
AC P0A2G4; P24115;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Citrate-proton symporter;
DE AltName: Full=Citrate carrier protein;
DE AltName: Full=Citrate transporter;
DE AltName: Full=Citrate utilization determinant;
DE AltName: Full=Citrate utilization protein A;
GN Name=citA; OrderedLocusNames=STY0727, t2186;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Uptake of citrate across the boundary membrane with the
CC concomitant transport of protons into the cell (symport system).
CC {ECO:0000250|UniProtKB:P0A2G3}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Allows the utilization of citrate as a sole source of
CC carbon and energy. {ECO:0000250|UniProtKB:P0A2G3}.
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; AL513382; CAD05152.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69796.1; -; Genomic_DNA.
DR RefSeq; NP_455250.1; NC_003198.1.
DR RefSeq; WP_000057014.1; NZ_WSUR01000015.1.
DR AlphaFoldDB; P0A2G4; -.
DR SMR; P0A2G4; -.
DR STRING; 220341.16501925; -.
DR EnsemblBacteria; AAO69796; AAO69796; t2186.
DR KEGG; stt:t2186; -.
DR KEGG; sty:STY0727; -.
DR PATRIC; fig|220341.7.peg.732; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_39_0_6; -.
DR OMA; MYGIYNG; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 GO; GO:0006101; P:citrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004736; MHS_symport.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00883; 2A0106; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Citrate utilization; Membrane; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..434
FT /note="Citrate-proton symporter"
FT /id="PRO_0000050299"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..54
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..111
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..335
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..400
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 434 AA; 47189 MW; E0F077EAC70DB444 CRC64;
MAQHTPATSR AGTFGAILRV TSGNFLEQFD FFLFGFYATY IARTFFPAES EFASLMLTFA
VFGSGFLMRP VGAIVLGAYI DRIGRRKGLM VTLAIMGCGT LLIALVPGYQ TIGLAAPALV
LLGRLLQGFS AGVELGGVSV YLSEIATPGN KGFYTSWQSA SQQVAIVVAA LIGYSLNITL
GHDAISEWGW RIPFFIGCMI IPLIFVLRRS LQETEAFLQR KHRPDTREIF ATIAKNWRII
TAGTLLVAMT TTTFYFITVY TPTYGRTVLN LSARDSLIVT MLVGVSNFIW LPIGGAISDR
IGRRAVLMGI TLLALITTWP VMQWLTAAPD FTRMTLVLLW FSFFFGMYNG AMVAALTEVM
PVYVRTVGFS LAFSLATAIF GGLTPAISTA LVKLTGDKSS PGWWLMCAAL CGLAATAMLF
VRLSRGYIAA ENKA
