CITN_BACSU
ID CITN_BACSU Reviewed; 426 AA.
AC P42308;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Citrate transporter;
GN Name=citN; Synonyms=citH, yxiQ; OrderedLocusNames=BSU39060; ORFNames=N15CR;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 95; 123; 157 AND 311-312.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 330-426.
RC STRAIN=168;
RX PubMed=7704256; DOI=10.1099/13500872-141-2-281;
RA Wolf M., Geczi A., Simon O., Borriss R.;
RT "Genes encoding xylan and beta-glucan hydrolysing enzymes in Bacillus
RT subtilis: characterization, mapping and construction of strains deficient
RT in lichenase, cellulase and xylanase.";
RL Microbiology 141:281-290(1995).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8892821; DOI=10.1128/jb.178.21.6216-6222.1996;
RA Boorsma A., van der Rest M.E., Lolkema J.S., Konings W.N.;
RT "Secondary transporters for citrate and the Mg(2+)-citrate complex in
RT Bacillus subtilis are homologous proteins.";
RL J. Bacteriol. 178:6216-6222(1996).
CC -!- FUNCTION: Transports the free citrate anion. Probably cotransports
CC citrate and at least three or four protons. The citrate uptake is
CC inhibited by the presence of magnesium ions.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D83026; BAA11698.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15932.2; -; Genomic_DNA.
DR EMBL; Z46862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D70078; D70078.
DR RefSeq; NP_391785.2; NC_000964.3.
DR RefSeq; WP_003227205.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42308; -.
DR SMR; P42308; -.
DR STRING; 224308.BSU39060; -.
DR TCDB; 2.A.11.1.2; the citrate-mg(2+):h(+) (citm) citrate-ca(2+):h(+) (cith) symporter (citmhs) family.
DR PaxDb; P42308; -.
DR PRIDE; P42308; -.
DR EnsemblBacteria; CAB15932; CAB15932; BSU_39060.
DR GeneID; 937469; -.
DR KEGG; bsu:BSU39060; -.
DR PATRIC; fig|224308.179.peg.4229; -.
DR eggNOG; COG2851; Bacteria.
DR InParanoid; P42308; -.
DR OMA; FMSNDGF; -.
DR PhylomeDB; P42308; -.
DR BioCyc; BSUB:BSU39060-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR014738; Citrate_transporter.
DR Pfam; PF03600; CitMHS; 1.
DR TIGRFAMs; TIGR00784; citMHS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Citrate utilization; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Citrate transporter"
FT /id="PRO_0000089775"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 95
FT /note="L -> F (in Ref. 1; BAA11698)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> R (in Ref. 1; BAA11698)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> E (in Ref. 1; BAA11698)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="LV -> TR (in Ref. 1; BAA11698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 45300 MW; 83B147441CF46D2D CRC64;
MLAILGFVMM IVFMYLIMSN RLSALIALIV VPIVFALISG FGKDLGEMMI QGVTDLAPTG
IMLLFAILYF GIMIDSGLFD PLIAKILSFV KGDPLKIAVG TAVLTMTISL DGDGTTTYMI
TIAAMLPLYK RLGMNRLVLA GIAMLGSGVM NIIPWGGPTA RVLASLKLDT SEVFTPLIPA
MIAGILWVIA VAYILGKKER KRLGVISIDH APSSDPEAAP LKRPALQWFN LLLTVALMAA
LITSLLPLPV LFMTAFAVAL MVNYPNVKEQ QKRISAHAGN ALNVVSMVFA AGIFTGILSG
TKMVDAMAHS LVSLIPDAMG PHLPLITAIV SMPFTFFMSN DAFYFGVLPI IAEAASAYGI
DAAEIGRASL LGQPVHLLSP LVPSTYLLVG MAGVSFGDHQ KFTIKWAVGT TIVMTIAALL
IGIISF