TTRB_SALTY
ID TTRB_SALTY Reviewed; 250 AA.
AC Q7CQM9; Q7B2G3; Q7BK19;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tetrathionate reductase subunit B;
DE AltName: Full=Tetrathionate reductase electron transport protein;
DE Flags: Precursor;
GN Name=ttrB; OrderedLocusNames=STM1385;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=10027966; DOI=10.1046/j.1365-2958.1999.01190.x;
RA Hensel M., Egelseer C., Nikolaus T.;
RT "Molecular and functional analysis indicates a mosaic structure of
RT Salmonella pathogenicity island 2.";
RL Mol. Microbiol. 31:489-498(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=11274105; DOI=10.1128/jb.183.8.2463-2475.2001;
RA Price-Carter M., Tingey J., Bobik T.A., Roth J.R.;
RT "The alternative electron acceptor tetrathionate supports B12-dependent
RT anaerobic growth of Salmonella enterica serovar typhimurium on ethanolamine
RT or 1,2-propanediol.";
RL J. Bacteriol. 183:2463-2475(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10231485; DOI=10.1046/j.1365-2958.1999.01345.x;
RA Hensel M., Hinsley A.P., Nikolaus T., Sawers G., Berks B.C.;
RT "The genetic basis of tetrathionate respiration in Salmonella
RT typhimurium.";
RL Mol. Microbiol. 32:275-287(1999).
RN [5]
RP FUNCTION IN VIRULENCE.
RX PubMed=20864996; DOI=10.1038/nature09415;
RA Winter S.E., Thiennimitr P., Winter M.G., Butler B.P., Huseby D.L.,
RA Crawford R.W., Russell J.M., Bevins C.L., Adams L.G., Tsolis R.M.,
RA Roth J.R., Baumler A.J.;
RT "Gut inflammation provides a respiratory electron acceptor for
RT Salmonella.";
RL Nature 467:426-429(2010).
CC -!- FUNCTION: Part of a membrane-bound tetrathionate reductase that
CC catalyzes the reduction of tetrathionate to thiosulfate. TtrB is
CC probably involved in transfer of electrons from TtrC to TtrA. During
CC mice infection, the ability to use tetrathionate as an electron
CC acceptor is a growth advantage for S.typhimurium over the competing
CC microbiota in the lumen of the inflamed gut.
CC {ECO:0000269|PubMed:10231485, ECO:0000269|PubMed:20864996}.
CC -!- SUBUNIT: Probably composed of three subunits: TtrA, TtrB and TtrC.
CC {ECO:0000269|PubMed:10231485}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10231485}. Cell
CC inner membrane {ECO:0000305|PubMed:10231485}; Peripheral membrane
CC protein {ECO:0000305|PubMed:10231485}; Periplasmic side
CC {ECO:0000305|PubMed:10231485}.
CC -!- INDUCTION: Transcriptionally regulated by Fnr and by the TtrR/TtrS two-
CC component regulatory system. {ECO:0000269|PubMed:10231485,
CC ECO:0000269|PubMed:11274105}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
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DR EMBL; AJ224978; CAB37414.1; -; Genomic_DNA.
DR EMBL; AF282268; AAG31757.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20309.1; -; Genomic_DNA.
DR RefSeq; NP_460350.1; NC_003197.2.
DR RefSeq; WP_000269830.1; NC_003197.2.
DR AlphaFoldDB; Q7CQM9; -.
DR SMR; Q7CQM9; -.
DR STRING; 99287.STM1385; -.
DR PaxDb; Q7CQM9; -.
DR DNASU; 1252903; -.
DR EnsemblBacteria; AAL20309; AAL20309; STM1385.
DR GeneID; 1252903; -.
DR KEGG; stm:STM1385; -.
DR PATRIC; fig|99287.12.peg.1468; -.
DR HOGENOM; CLU_043374_1_3_6; -.
DR OMA; VSCSMEN; -.
DR PhylomeDB; Q7CQM9; -.
DR BioCyc; MetaCyc:MON-12550; -.
DR BioCyc; SENT99287:STM1385-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Periplasm; Reference proteome;
KW Repeat; Signal; Transport.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..250
FT /note="Tetrathionate reductase subunit B"
FT /id="PRO_0000417418"
FT DOMAIN 50..79
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 97..128
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 129..158
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 27710 MW; 8B40C8868DA05763 CRC64;
MWTGVNMDSS KRQFLQQLGV LTAGASLVPL AEAKFPFSPE RHEGSPRHRY AMLIDLRRCI
GCQSCTVSCT IENQTPQGAF RTTVNQYQVQ REGSQEVTNV LLPRLCNHCD NPPCVPVCPV
QATFQREDGI VVVDNKRCVG CAYCVQACPY DARFINHETQ TADKCTFCVH RLEAGLLPAC
VESCVGGARI IGDIKDPHSR IATMLHQHRD AIKVLKPENG TSPHVFYLGL DDAFVTPLMG
RAQPALWQEV
