TAUA_ECOLI
ID TAUA_ECOLI Reviewed; 320 AA.
AC Q47537; P77630; Q2MC60;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Taurine-binding periplasmic protein;
DE AltName: Full=Sulfate starvation-induced protein 1;
DE Short=SSI1;
DE Flags: Precursor;
GN Name=tauA; Synonyms=ssiA, yaiR; OrderedLocusNames=b0365, JW0357;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
CC -!- FUNCTION: Part of a binding-protein-dependent transport system for
CC taurine.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by sulfate or cysteine.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein SsuA/TauA
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18088.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D85613; BAA12838.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18088.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73468.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76146.1; -; Genomic_DNA.
DR PIR; S78604; S78604.
DR RefSeq; NP_414899.2; NC_000913.3.
DR RefSeq; WP_001018417.1; NZ_LN832404.1.
DR PDB; 6SSY; X-ray; 1.62 A; A/B=22-319.
DR PDB; 6ST0; X-ray; 1.50 A; A/B=22-319.
DR PDB; 6ST1; X-ray; 1.55 A; A/B=22-319.
DR PDB; 6STL; X-ray; 1.30 A; A/B=22-319.
DR PDBsum; 6SSY; -.
DR PDBsum; 6ST0; -.
DR PDBsum; 6ST1; -.
DR PDBsum; 6STL; -.
DR AlphaFoldDB; Q47537; -.
DR SMR; Q47537; -.
DR BioGRID; 4261088; 25.
DR ComplexPortal; CPX-4312; Taurine ABC transporter complex.
DR IntAct; Q47537; 1.
DR STRING; 511145.b0365; -.
DR TCDB; 3.A.1.17.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q47537; -.
DR PRIDE; Q47537; -.
DR EnsemblBacteria; AAC73468; AAC73468; b0365.
DR EnsemblBacteria; BAE76146; BAE76146; BAE76146.
DR GeneID; 945030; -.
DR KEGG; ecj:JW0357; -.
DR KEGG; eco:b0365; -.
DR PATRIC; fig|1411691.4.peg.1914; -.
DR EchoBASE; EB3085; -.
DR eggNOG; COG4521; Bacteria.
DR HOGENOM; CLU_028871_3_1_6; -.
DR InParanoid; Q47537; -.
DR OMA; FIWDPVL; -.
DR PhylomeDB; Q47537; -.
DR BioCyc; EcoCyc:TAUA-MON; -.
DR BioCyc; MetaCyc:TAUA-MON; -.
DR PRO; PR:Q47537; -.
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:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0042959; F:alkanesulfonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042918; P:alkanesulfonate transport; IBA:GO_Central.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP:EcoCyc.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IC:ComplexPortal.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
DR GO; GO:0015734; P:taurine transport; IMP:EcoCyc.
DR CDD; cd13560; PBP2_taurine; 1.
DR InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR InterPro; IPR010068; Peri-bd_TauA.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR30024:SF38; PTHR30024:SF38; 1.
DR Pfam; PF04069; OpuAC; 1.
DR SMART; SM00062; PBPb; 1.
DR TIGRFAMs; TIGR01729; taurine_ABC_bnd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..22
FT CHAIN 23..320
FT /note="Taurine-binding periplasmic protein"
FT /id="PRO_0000031865"
FT CONFLICT 62..63
FT /note="AS -> SA (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="R -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Q -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:6STL"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:6STL"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6STL"
SQ SEQUENCE 320 AA; 34266 MW; B07D54A1D2B5BE55 CRC64;
MAISSRNTLL AALAFIAFQA QAVNVTVAYQ TSAEPAKVAQ ADNTFAKESG ATVDWRKFDS
GASIVRALAS GDVQIGNLGS SPLAVAASQQ VPIEVFLLAS KLGNSEALVV KKTISKPEDL
IGKRIAVPFI STTHYSLLAA LKHWGIKPGQ VEIVNLQPPA IIAAWQRGDI DGAYVWAPAV
NALEKDGKVL TDSEQVGQWG APTLDVWVVR KDFAEKHPEV VKAFAKSAID AQQPYIANPD
VWLKQPENIS KLARLSGVPE GDVPGLVKGN TYLTPQQQTA ELTGPVNKAI IDTAQFLKEQ
GKVPAVANDY SQYVTSRFVQ
