TTRC_SALTY
ID TTRC_SALTY Reviewed; 340 AA.
AC Q9Z4S7; Q7BK18; Q7CQN0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Tetrathionate reductase subunit C;
GN Name=ttrC; OrderedLocusNames=STM1384;
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 [GENOMIC DNA].
RC STRAIN=51K61;
RX PubMed=15574899; DOI=10.1128/aem.70.12.7046-7052.2004;
RA Malorny B., Paccassoni E., Fach P., Bunge C., Martin A., Helmuth R.;
RT "Diagnostic real-time PCR for detection of Salmonella in food.";
RL Appl. Environ. Microbiol. 70:7046-7052(2004).
RN [4]
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 [5]
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 [6]
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. TtrC probably
CC anchors TtrA and TtrB to the periplasmic face of the cytoplasmic
CC membrane. May transfer electrons from membrane quinol to TtrB. 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: Cell inner membrane
CC {ECO:0000305|PubMed:10231485}; Multi-pass membrane protein
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 -!- SIMILARITY: Belongs to the NrfD family. {ECO:0000305}.
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DR EMBL; AJ224978; CAB37415.1; -; Genomic_DNA.
DR EMBL; AF282268; AAG31758.1; -; Genomic_DNA.
DR EMBL; AY578064; AAS90304.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20308.1; -; Genomic_DNA.
DR RefSeq; NP_460349.1; NC_003197.2.
DR RefSeq; WP_000149760.1; NC_003197.2.
DR AlphaFoldDB; Q9Z4S7; -.
DR SMR; Q9Z4S7; -.
DR STRING; 99287.STM1384; -.
DR PaxDb; Q9Z4S7; -.
DR EnsemblBacteria; AAL20308; AAL20308; STM1384.
DR GeneID; 1252902; -.
DR KEGG; stm:STM1384; -.
DR PATRIC; fig|99287.12.peg.1467; -.
DR HOGENOM; CLU_061956_0_0_6; -.
DR BioCyc; MetaCyc:MON-12551; -.
DR BioCyc; SENT99287:STM1384-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR InterPro; IPR005614; NrfD_fam.
DR Pfam; PF03916; NrfD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Tetrathionate reductase subunit C"
FT /id="PRO_0000417420"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 340 AA; 38395 MW; E26B775FE2A671CC CRC64;
MTHSLIIEEV LAHPQDISWL PWAVQYFFFI GIAACAALFA CYLHWRKKDA ATEENRALLI
AITCAITAPL ALTADLHQTA RVWHFYAWPT PWSWMPWGAL FLPLFTGFLA LWFLAQQIKR
LFNKSYNVTK WLALASALCA VGLLIYTGRE VSVVLARPIW FSYAFPVAMF LSALQAFFAL
MIVAARRDSV RLPKILWGQI WTLAALGLVV AMWVSGDTLS GTAIRQWITV ALSAKYYAVG
WVALWVCTLL FCSLALRHPL SQLRRVLLVL SALALCWLMR WTLLIQVQTV PKFNAQFNPY
SLPGGTDGWL AILGTFGLWI ALLIIIRETL NGLTRRLQHG
