ID   CAIT_ECOLC              Reviewed;         504 AA.
AC   B1IRD6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN   Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=EcolC_3615;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79229.1; -; Genomic_DNA.
DR   RefSeq; WP_000787109.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IRD6; -.
DR   SMR; B1IRD6; -.
DR   KEGG; ecl:EcolC_3615; -.
DR   HOGENOM; CLU_010118_6_0_6; -.
DR   OMA; AWAPFTG; -.
DR   UniPathway; UPA00117; -.
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..504
FT                   /note="L-carnitine/gamma-butyrobetaine antiporter"
FT                   /id="PRO_1000084421"
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;  56605 MW;  AD4632D9B8622D82 CRC64;
     MKNEKRKTGI EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
     VMLFGWFWLV FGPYAKKRLG NEPPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
     FGLEPNSTGA KELGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMEVIR PSSTLVPLVG
     EKHAKGLFGT IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
     ILNAICVACG LQKGVRIASD VRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMYLPRM
     LFYTDPIAKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVLGLTASTW
     ILWTVLGSNT LLLMDKNIIN IPNLIEQYGV ARAIIETWAA LPLSTATMWG FFILCFIATV
     TLVNACSYTL AMSTCREVRD GEEPPLLVRI GWSILVGIIG IVLLALGGLK PIQTAIIAGG
     CPLFFVNIMV TLSFIKDAKQ NWKD