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Database: UniProt
Entry: CAIT_SALTY
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ID   CAIT_SALTY              Reviewed;         505 AA.
AC   Q8ZRX1;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN   Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=STM0074;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19038.1; -; Genomic_DNA.
DR   RefSeq; NP_459079.1; NC_003197.2.
DR   RefSeq; WP_000787073.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRX1; -.
DR   SMR; Q8ZRX1; -.
DR   STRING; 99287.STM0074; -.
DR   PaxDb; 99287-STM0074; -.
DR   GeneID; 1251592; -.
DR   KEGG; stm:STM0074; -.
DR   PATRIC; fig|99287.12.peg.76; -.
DR   HOGENOM; CLU_010118_6_0_6; -.
DR   PhylomeDB; Q8ZRX1; -.
DR   BioCyc; SENT99287:STM0074-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0044667; F:(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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   NCBIfam; TIGR00842; bcct; 1.
DR   PANTHER; PTHR30047; HIGH-AFFINITY CHOLINE TRANSPORT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30047:SF11; L-CARNITINE_GAMMA-BUTYROBETAINE ANTIPORTER; 1.
DR   Pfam; PF02028; BCCT; 1.
DR   PROSITE; PS01303; BCCT; 1.
PE   3: Inferred from homology;
KW   Antiport; Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..505
FT                   /note="L-carnitine/gamma-butyrobetaine antiporter"
FT                   /id="PRO_0000201491"
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;  56643 MW;  0E678698707F9665 CRC64;
     MKNEKKKSGI EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
     VMLFGWFWLV FGPYAKKRLG DEKPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
     FGLEPNSTGA KEIGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMDVIR PSSTLVPLVG
     EKHAKGLFGT 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
//
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