ID   CAIT_SHIDS              Reviewed;         504 AA.
AC   Q32K57;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN   Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=SDY_0062;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB60300.1; -; Genomic_DNA.
DR   RefSeq; WP_000787133.1; NC_007606.1.
DR   RefSeq; YP_401789.1; NC_007606.1.
DR   AlphaFoldDB; Q32K57; -.
DR   SMR; Q32K57; -.
DR   STRING; 300267.SDY_0062; -.
DR   EnsemblBacteria; ABB60300; ABB60300; SDY_0062.
DR   KEGG; sdy:SDY_0062; -.
DR   PATRIC; fig|300267.13.peg.68; -.
DR   HOGENOM; CLU_010118_6_0_6; -.
DR   OMA; AWAPFTG; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000002716; 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; IPR000060; BCCT_transptr.
DR   InterPro; IPR023449; BCCT_transptr_CaiT.
DR   PANTHER; PTHR30047; PTHR30047; 1.
DR   Pfam; PF02028; BCCT; 1.
DR   TIGRFAMs; TIGR00842; 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..504
FT                   /note="L-carnitine/gamma-butyrobetaine antiporter"
FT                   /id="PRO_1000064335"
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        398..418
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   504 AA;  56432 MW;  3453EC8384857668 CRC64;
     MKNEKRKTGM EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
     VMLFGWFWLV FGPYAKKRLG NEPPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
     FGLEPNSTGA KELGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMEVIR PSSTLVPLVG
     EKHAKGLFGT IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
     ILNAICVACG LQKGGRIASD VPSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMYLPRM
     LFYTDPIAKG GFPQGWSVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVLGLTASTW
     ILWTVLGSNT LLLIDKNIIN IPNLIEQYGV ARAIIETWAA LPLSTATMWG FFILCFIATV
     TLVNACSYTL AMSTCREVRG GEEPPLLVRI GWSILVGIIG IVLLALGGLK PIQTAIIAGG
     CPLFFVNIMV TLSFIKDAKQ NWKD