BETT_ECOLI
ID BETT_ECOLI Reviewed; 677 AA.
AC P0ABC9; P17447; Q2MCA9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=High-affinity choline transport protein {ECO:0000305};
GN Name=betT {ECO:0000303|PubMed:1956285}; OrderedLocusNames=b0314, JW0306;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1956285; DOI=10.1111/j.1365-2958.1991.tb01877.x;
RA Lamark T., Kaasen E., Eshoo M.W., Falkenberg P., McDougall J., Strom A.R.;
RT "DNA sequence and analysis of the bet genes encoding the osmoregulatory
RT choline-glycine betaine pathway of Escherichia coli.";
RL Mol. Microbiol. 5:1049-1064(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: High-affinity uptake of choline driven by a proton-motive
CC force. {ECO:0000269|PubMed:1956285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline(in) + H(+)(in) = choline(out) + H(+)(out);
CC Xref=Rhea:RHEA:28843, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:1956285};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28845;
CC Evidence={ECO:0000269|PubMed:1956285};
CC -!- ACTIVITY REGULATION: The choline uptake activity is completely
CC inhibited by the protonophore carbonyl cyanide 4-
CC (trifluoromethoxy)phenylhydrazone (FCCP). {ECO:0000269|PubMed:1956285}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By osmotic stress. Choline is required for full expression.
CC {ECO:0000269|PubMed:1956285}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; X52905; CAA37090.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18040.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73417.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76097.1; -; Genomic_DNA.
DR PIR; S15179; S15179.
DR RefSeq; NP_414848.1; NC_000913.3.
DR RefSeq; WP_000131044.1; NZ_STEB01000020.1.
DR AlphaFoldDB; P0ABC9; -.
DR SMR; P0ABC9; -.
DR BioGRID; 4262802; 218.
DR STRING; 511145.b0314; -.
DR TCDB; 2.A.15.1.4; the betaine/carnitine/choline transporter (bcct) family.
DR PaxDb; P0ABC9; -.
DR PRIDE; P0ABC9; -.
DR EnsemblBacteria; AAC73417; AAC73417; b0314.
DR EnsemblBacteria; BAE76097; BAE76097; BAE76097.
DR GeneID; 66671386; -.
DR GeneID; 945079; -.
DR KEGG; ecj:JW0306; -.
DR KEGG; eco:b0314; -.
DR PATRIC; fig|1411691.4.peg.1963; -.
DR EchoBASE; EB0110; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_3_1_6; -.
DR InParanoid; P0ABC9; -.
DR OMA; WAMYALM; -.
DR PhylomeDB; P0ABC9; -.
DR BioCyc; EcoCyc:BETT-MON; -.
DR BioCyc; MetaCyc:BETT-MON; -.
DR UniPathway; UPA00529; -.
DR PRO; PR:P0ABC9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR InterPro; IPR018093; BCCT_CS.
DR InterPro; IPR000060; BCCT_transptr.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..677
FT /note="High-affinity choline transport protein"
FT /id="PRO_0000201484"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 677 AA; 75842 MW; 76062FCE877D0A55 CRC64;
MTDLSHSREK DKINPVVFYT SAGLILLFSL TTILFRDFSA LWIGRTLDWV SKTFGWYYLL
AATLYIVFVV CIACSRFGSV KLGPEQSKPE FSLLSWAAML FAAGIGIDLM FFSVAEPVTQ
YMQPPEGAGQ TIEAARQAMV WTLFHYGLTG WSMYALMGMA LGYFSYRYNL PLTIRSALYP
IFGKRINGPI GHSVDIAAVI GTIFGIATTL GIGVVQLNYG LSVLFDIPDS MAAKAALIAL
SVIIATISVT SGVDKGIRVL SELNVALALG LILFVLFMGD TSFLLNALVL NVGDYVNRFM
GMTLNSFAFD RPVEWMNNWT LFFWAWWVAW SPFVGLFLAR ISRGRTIRQF VLGTLIIPFT
FTLLWLSVFG NSALYEIIHG GAAFAEEAMV HPERGFYSLL AQYPAFTFSA SVATITGLLF
YVTSADSGAL VLGNFTSQLK DINSDAPGWL RVFWSVAIGL LTLGMLMTNG ISALQNTTVI
MGLPFSFVIF FVMAGLYKSL KVEDYRRESA NRDTAPRPLG LQDRLSWKKR LSRLMNYPGT
RYTKQMMETV CYPAMEEVAQ ELRLRGAYVE LKSLPPEEGQ QLGHLDLLVH MGEEQNFVYQ
IWPQQYSVPG FTYRARSGKS TYYRLETFLL EGSQGNDLMD YSKEQVITDI LDQYERHLNF
IHLHREAPGH SVMFPDA
