CAIT_SALTI
ID CAIT_SALTI Reviewed; 505 AA.
AC Q8Z9L1;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049};
GN OrderedLocusNames=STY0084, t0075;
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: Catalyzes the exchange of L-carnitine for gamma-
CC butyrobetaine. {ECO:0000255|HAMAP-Rule:MF_01049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + 4-(trimethylamino)butanoate(in) = (R)-
CC carnitine(in) + 4-(trimethylamino)butanoate(out);
CC Xref=Rhea:RHEA:29427, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01049};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01049}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01049}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01049}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01049}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family. CaiT
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01049}.
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DR EMBL; AL513382; CAD01228.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67808.1; -; Genomic_DNA.
DR RefSeq; NP_454684.1; NC_003198.1.
DR RefSeq; WP_000787084.1; NZ_WSUR01000028.1.
DR AlphaFoldDB; Q8Z9L1; -.
DR SMR; Q8Z9L1; -.
DR STRING; 220341.16501357; -.
DR EnsemblBacteria; AAO67808; AAO67808; t0075.
DR KEGG; stt:t0075; -.
DR KEGG; sty:STY0084; -.
DR PATRIC; fig|220341.7.peg.83; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_6_0_6; -.
DR OMA; AWAPFTG; -.
DR UniPathway; UPA00117; -.
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:0044667; F:(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity; IEA:InterPro.
DR GO; GO:1900751; P:4-(trimethylammonio)butanoate transport; IEA:InterPro.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01049; CaiT; 1.
DR InterPro; IPR018093; BCCT_CS.
DR InterPro; IPR000060; BCCT_transptr.
DR InterPro; IPR023449; BCCT_transptr_CaiT.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..505
FT /note="L-carnitine/gamma-butyrobetaine antiporter"
FT /id="PRO_0000201490"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01049"
SQ SEQUENCE 505 AA; 56748 MW; 43D41A070CBEB108 CRC64;
MKNEKRKSGI EPKVFFPLLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
VMLFSWFWLV FGPYAKKRLG DEKPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
FGLEPNSTGA KEIGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMDVIR PSSTLVPLVG
EKHAKGLFST IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
ILNAICVACG LQKGVRIASD VRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMHLPRM
LFYTDAIGKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVMGLTASTW
ILWTVLGSNT LLLMDKNILN IPQLIEQHGV ARAIIETWAA LPLSTATMWG FFILCFIATV
TLINACSYTL AMSTCREVRD GEEPPLLVRI GWSVLVGIIG IVLLALGGLK PIQTAIIAGG
CPLFFVNIMV TLSFIKDAKV HWKDK
