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CAIT_SALG2
ID   CAIT_SALG2              Reviewed;         505 AA.
AC   B5RGA7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN   Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=SG0077;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR35984.1; -; Genomic_DNA.
DR   RefSeq; WP_000787068.1; NC_011274.1.
DR   AlphaFoldDB; B5RGA7; -.
DR   SMR; B5RGA7; -.
DR   EnsemblBacteria; CAR35984; CAR35984; SG0077.
DR   KEGG; seg:SG0077; -.
DR   HOGENOM; CLU_010118_6_0_6; -.
DR   OMA; AWAPFTG; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008321; 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_1000136240"
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;  56700 MW;  28C3F4BC5A2DFE2D 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 VRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMHLPRM
     LFYTDAIGKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVMGLTASTW
     ILWTVLGSNT LLLMDKNILN IPQLIEQHVV ARAIIETWAA LPLSTATMWG FFILCFIATV
     TLINACSYTL AMSTCREVRD GEEPPLLVRI GWSVLVGIIG IVLLALGGLK PIQTAIIAGG
     CPLFFVNIMV TLSFIKDAKV HWKDK
 
 
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