CAIT_SHIFL
ID CAIT_SHIFL Reviewed; 504 AA.
AC P59335;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=L-carnitine/gamma-butyrobetaine antiporter {ECO:0000255|HAMAP-Rule:MF_01049};
GN Name=caiT {ECO:0000255|HAMAP-Rule:MF_01049};
GN OrderedLocusNames=SF0037, S0039;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41703.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15584.1; -; Genomic_DNA.
DR RefSeq; NP_705996.1; NC_004337.2.
DR RefSeq; WP_000787092.1; NZ_WPGW01000005.1.
DR AlphaFoldDB; P59335; -.
DR SMR; P59335; -.
DR STRING; 198214.SF0037; -.
DR EnsemblBacteria; AAN41703; AAN41703; SF0037.
DR EnsemblBacteria; AAP15584; AAP15584; S0039.
DR GeneID; 1024556; -.
DR KEGG; sfl:SF0037; -.
DR KEGG; sfx:S0039; -.
DR PATRIC; fig|198214.7.peg.43; -.
DR HOGENOM; CLU_010118_6_0_6; -.
DR OMA; AWAPFTG; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="L-carnitine/gamma-butyrobetaine antiporter"
FT /id="PRO_0000201492"
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; 56595 MW; 65B839C3E252F134 CRC64;
MKNEKRKTGI EPKVFFPPLI IVGILCWLTV RDLDAANVVI NAVFSYVTNV WGWAFEWYMV
VMLFGWFWLV FGPYAKKRLG NEPPEFSTAS WIFMMFASCT SAAVLFWGSI EIYYYISTPP
FGLEPNSTGA KELGLAYSLF HWGPLPWATY SFLSVAFAYF FFVRKMEVIR PSSTLVPLAG
EKHAKGLFGT IVDNFYLVAL IFAMGTSLGL ATPLVTECMQ WLFGIPHTLQ LDAIIITCWI
ILNAICVACG LQKGVRIASD VRSYLSFLML GWVFIVSGAS FIMNYFTDSV GMLLMYLPRM
LFYTDPIAKG GFPQGWTVFY WAWWVIYAIQ MSIFLARISR GRTVRELCFG MVMGLTASTW
ILWTVLGSNT LLLMDKNIIN IPNLIEQYGV ARAIIETWAA LPLSTATMWG FFILCFIATV
TLVNACSYTL AMSTCREVRD GEEPPLLVRI GWSILVGIIG IVLLALGGLK PIQTAIIAGG
CPLFFVNIMV TLSFIKDAKQ NWKD
