ID   CAIT_SALPA              Reviewed;         505 AA.
AC   Q5PIN5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN   Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=SPA0075;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76109.1; -; Genomic_DNA.
DR   RefSeq; WP_000787067.1; NC_006511.1.
DR   AlphaFoldDB; Q5PIN5; -.
DR   SMR; Q5PIN5; -.
DR   EnsemblBacteria; AAV76109; AAV76109; SPA0075.
DR   KEGG; spt:SPA0075; -.
DR   HOGENOM; CLU_010118_6_0_6; -.
DR   OMA; AWAPFTG; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008185; 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_1000064334"
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;  56690 MW;  7793E5BC52CB38F6 CRC64;
     MKNEKKKSGI EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMI
     VMLFGWFWLV FGPYAKKRLG DEKPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
     FGLEPNSTGA KEIGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMDVIR PSSTLVPLVG
     EKHAKGLFGT IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
     ILNAICVACG LQKGVRIASD MRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMHLPRM
     LFYTDAIGKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVMGLTASTW
     ILWTVLGSNT LLLMDKNILN IPQLIEQHGV ARAIIETWAA LPLSTATMWG FFILCFIATV
     TLINACSYTL AMSTCREVRD GEEPPLLVRI GWSVLVGIIG IVLLALGGLK PIQTAIIAGG
     CPLFFVNIMV TLSFIKDAKV HWKDK