TTRA_SALTY
ID TTRA_SALTY Reviewed; 1020 AA.
AC Q9Z4S6; Q7BK17; Q7CQN1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tetrathionate reductase subunit A;
DE EC=1.8.-.-;
DE AltName: Full=Tetrathionate reductase molybdenum subunit;
DE Flags: Precursor;
GN Name=ttrA; OrderedLocusNames=STM1383;
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, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
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. TtrA is the
CC catalytic subunit. During mice infection, the ability to use
CC tetrathionate as an electron acceptor is a growth advantage for
CC S.typhimurium over the competing microbiota in the lumen of the
CC inflamed gut. {ECO:0000269|PubMed:10231485,
CC ECO:0000269|PubMed:20864996}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
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.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in tetrathionate
CC respiration. {ECO:0000269|PubMed:10231485}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ224978; CAB37416.1; -; Genomic_DNA.
DR EMBL; AF282268; AAG31759.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20307.1; -; Genomic_DNA.
DR RefSeq; NP_460348.1; NC_003197.2.
DR RefSeq; WP_000002375.1; NC_003197.2.
DR AlphaFoldDB; Q9Z4S6; -.
DR STRING; 99287.STM1383; -.
DR PaxDb; Q9Z4S6; -.
DR EnsemblBacteria; AAL20307; AAL20307; STM1383.
DR GeneID; 1252901; -.
DR KEGG; stm:STM1383; -.
DR PATRIC; fig|99287.12.peg.1466; -.
DR HOGENOM; CLU_008235_0_0_6; -.
DR OMA; ERYSGCP; -.
DR PhylomeDB; Q9Z4S6; -.
DR BioCyc; MetaCyc:MON-12549; -.
DR BioCyc; SENT99287:STM1383-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR CDD; cd02758; MopB_Tetrathionate-Ra; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR041929; Tetrathionate-R_A_N.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 34..1020
FT /note="Tetrathionate reductase subunit A"
FT /id="PRO_0000417416"
FT DOMAIN 71..154
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 1020 AA; 110993 MW; 19CC5E9BF4EDF269 CRC64;
MANLTRRQWL KVGLAVGGMV TFGLSYRDVA KRAIDGLLNG TSGKVTRDRI FGNALIPEAQ
AQTHWQQNPQ QTIAMTQCFG CWTQCGIRAR VNADGKVIRI AGNPYHPLSQ EHPIDSSVPF
SEAMEQLAGE SGLDARSTAC ARGATLLESL YSPLRLLEPM KRVGKRGEGK WQRISFEQLI
EEVVEGGDLF GEGHVDGLRA IHAPDTPIDA KHPSFGPKTN QLLVTNTSDE GRDAFLRRFA
LNSFGSKNFG AHGAYCGLAY RAGSGALMGD LDKNPHVKPD WENVEFALFM GTSPAQSGNP
FKRQARQLAS ARLRENFQYV VVAPALPLST VLADPRGRWQ PVMPGSDSAL AMGMIRWIMD
NQRYNADYLA IPGVQAMQQA GEQSWTNATH LVIADELPTL AGQHLTLRHL TPDGEETPVV
LNTDGELVDA STCRQARLFV TQYVTLADGQ RVTVKSGLQR LKEAAEKLSL AQYSEQCGVP
EAQIIALAET FTSHGRKAAV ISHGGMMAGN GFYNAWSVMM LNALIGNLSL SGGVFVGGGK
FNGVSDGPRY NMNSFAGKVK PSGLSIARSK TAYEASEEYR DKIAGGQSPY PAKAPWYPFV
AGQLTELLTS ALEGYPYPLK AWISNMSNPF YGVPGLRAVA EEKLKDPRRL PLFIAIDAFM
NETTALADYI VPDTHNFESW GFTAPWGGVA SKATTARWPV VAPATHRTAD GQPVSMEAFC
IAVAKRLHLP GFGDRAITDP QGNTFPLNRA EDFYLRVAAN IAFMGKTPVA LANQEDISLT
GVSRILPAIQ HTLKADEVGR VAFIYSRGGR FAPEDSGYTE QRLGNAWKKP LQIWNADVAA
HRHAITGERF SGCPVWYPAR LSDGRAIDDQ FPIGQWPLKL ISFKSNTMSS STAVIPRLHH
VKPANLVALN PQDGERYGLQ HGDRVRIITP GGQVVAQISL LNGVMPGVIA IEHGYGHREM
GATQHSLDGV PMPYDPQIRA GINLNDLGFA DPTRTITNTW LDWVSGAAVR QGLPAKIERI
