TAUB_ECOLI
ID TAUB_ECOLI Reviewed; 255 AA.
AC Q47538; Q2MC59;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Taurine import ATP-binding protein TauB {ECO:0000255|HAMAP-Rule:MF_01714};
DE EC=7.6.2.7 {ECO:0000255|HAMAP-Rule:MF_01714};
GN Name=tauB {ECO:0000255|HAMAP-Rule:MF_01714}; Synonyms=ssiB, yaiQ;
GN OrderedLocusNames=b0366, JW0358;
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, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=8808933; DOI=10.1128/jb.178.18.5438-5446.1996;
RA van der Ploeg J.R., Weiss M.A., Saller E., Nashimoto H., Saito N.,
RA Kertesz M.A., Leisinger T.;
RT "Identification of sulfate starvation-regulated genes in Escherichia coli:
RT a gene cluster involved in the utilization of taurine as a sulfur source.";
RL J. Bacteriol. 178:5438-5446(1996).
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 FUNCTION.
RX PubMed=10781534; DOI=10.1128/jb.182.10.2687-2695.2000;
RA Eichhorn E., van der Ploeg J.R., Leisinger T.;
RT "Deletion analysis of the Escherichia coli taurine and alkanesulfonate
RT transport systems.";
RL J. Bacteriol. 182:2687-2695(2000).
CC -!- FUNCTION: Part of the ABC transporter complex TauABC involved in
CC taurine import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01714, ECO:0000269|PubMed:10781534,
CC ECO:0000269|PubMed:8808933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurine(out) = ADP + H(+) + phosphate +
CC taurine(in); Xref=Rhea:RHEA:14613, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216, ChEBI:CHEBI:507393; EC=7.6.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01714};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TauB),
CC two transmembrane proteins (TauC) and a solute-binding protein (TauA).
CC {ECO:0000255|HAMAP-Rule:MF_01714}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01714}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01714}.
CC -!- INDUCTION: Regulated by CysB in response to sulfate starvation.
CC {ECO:0000269|PubMed:8808933}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Taurine
CC importer (TC 3.A.1.17.1) family. {ECO:0000255|HAMAP-Rule:MF_01714}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D85613; BAA12839.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18089.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73469.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76147.1; -; Genomic_DNA.
DR PIR; S78605; F64764.
DR RefSeq; NP_414900.1; NC_000913.3.
DR RefSeq; WP_000939375.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; Q47538; -.
DR SMR; Q47538; -.
DR BioGRID; 4261090; 8.
DR ComplexPortal; CPX-4312; Taurine ABC transporter complex.
DR IntAct; Q47538; 4.
DR STRING; 511145.b0366; -.
DR TCDB; 3.A.1.17.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q47538; -.
DR PRIDE; Q47538; -.
DR EnsemblBacteria; AAC73469; AAC73469; b0366.
DR EnsemblBacteria; BAE76147; BAE76147; BAE76147.
DR GeneID; 945027; -.
DR KEGG; ecj:JW0358; -.
DR KEGG; eco:b0366; -.
DR PATRIC; fig|1411691.4.peg.1913; -.
DR EchoBASE; EB3084; -.
DR eggNOG; COG4525; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; Q47538; -.
DR OMA; ALINCPK; -.
DR PhylomeDB; Q47538; -.
DR BioCyc; EcoCyc:TAUB-MON; -.
DR BioCyc; MetaCyc:TAUB-MON; -.
DR PRO; PR:Q47538; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IEP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015859; ABC_transpr_TauB.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42788:SF18; PTHR42788:SF18; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51250; TAUB; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..255
FT /note="Taurine import ATP-binding protein TauB"
FT /id="PRO_0000093007"
FT DOMAIN 2..229
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
SQ SEQUENCE 255 AA; 28297 MW; 12DDC6081CB7EA1B CRC64;
MLQISHLYAD YGGKPALEDI NLTLESGELL VVLGPSGCGK TTLLNLIAGF VPYQHGSIQL
AGKRIEGPGA ERGVVFQNEG LLPWRNVQDN VAFGLQLAGI EKMQRLEIAH QMLKKVGLEG
AEKRYIWQLS GGQRQRVGIA RALAANPQLL LLDEPFGALD AFTRDQMQTL LLKLWQETGK
QVLLITHDIE EAVFMATELV LLSSGPGRVL ERLPLNFARR FVAGESSRSI KSDPQFIAMR
EYVLSRVFEQ REAFS
