CAIT_ECO45
ID CAIT_ECO45 Reviewed; 504 AA.
AC B7MAG3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049}; OrderedLocusNames=ECS88_0043;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR01409.1; -; Genomic_DNA.
DR RefSeq; WP_000787103.1; NC_011742.1.
DR AlphaFoldDB; B7MAG3; -.
DR SMR; B7MAG3; -.
DR EnsemblBacteria; CAR01409; CAR01409; ECS88_0043.
DR KEGG; ecz:ECS88_0043; -.
DR HOGENOM; CLU_010118_6_0_6; -.
DR OMA; AWAPFTG; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000747; 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..504
FT /note="L-carnitine/gamma-butyrobetaine antiporter"
FT /id="PRO_1000136228"
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; 56587 MW; A852310DBEA22D82 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 LLLIDKNIIN IPNLIEQYGV ARAIIETWAA LPLSTATMWG FFILCFIATV
TLVNACSYTL AMSTCREVRD GEEPPLLVRI GWSILVGIIG IVLLALGGLK PIQTAIIAGG
CPLFFVNIMV TLSFIKDAKQ NWKD
