TTRS_SALTY
ID TTRS_SALTY Reviewed; 592 AA.
AC Q8ZPP6; Q9F7D6; Q9Z4S9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Tetrathionate sensor histidine kinase TtrS;
DE EC=2.7.13.3;
GN Name=ttrS; OrderedLocusNames=STM1386;
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 FUNCTION.
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, AND DISRUPTION 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: Member of the two-component regulatory system TtrR/TtrS,
CC which is required for synthesis of tetrathionate reductase. Probably
CC functions as a sensor protein kinase which is autophosphorylated at a
CC histidine residue in response to tetrathionate, and transfers its
CC phosphate group to TtrR. 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:11274105, ECO:0000269|PubMed:20864996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants are defective in tetrathionate
CC respiration. {ECO:0000269|PubMed:10231485}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG31756.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB37413.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ224978; CAB37413.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF282268; AAG31756.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20310.1; -; Genomic_DNA.
DR RefSeq; NP_460351.1; NC_003197.2.
DR RefSeq; WP_001214413.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPP6; -.
DR SMR; Q8ZPP6; -.
DR STRING; 99287.STM1386; -.
DR PaxDb; Q8ZPP6; -.
DR EnsemblBacteria; AAL20310; AAL20310; STM1386.
DR GeneID; 1252904; -.
DR KEGG; stm:STM1386; -.
DR PATRIC; fig|99287.12.peg.1469; -.
DR HOGENOM; CLU_011260_3_0_6; -.
DR OMA; MEKNKEW; -.
DR PhylomeDB; Q8ZPP6; -.
DR BioCyc; SENT99287:STM1386-MON; -.
DR BRENDA; 2.7.13.3; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..592
FT /note="Tetrathionate sensor histidine kinase TtrS"
FT /id="PRO_0000417422"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 364..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 367
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 592 AA; 65239 MW; F4179957B54DBE17 CRC64;
MRGKTVRRLA VLAAVGLLCH GAWAGTWNIG ILAMRGEAST RSHWQPLAKT LSQQLPGETF
HIQPLDLHQM QEAVNQGTVQ FVITNPAQFV QLNSHAPLRW LASLRSTRDG KAVSNVIGSV
ILTRRDSGIT TAHDLIGKTV GAIDAQAFGG YLLGYKALSD AGLRPERDFH LRFTGFPGDA
LVYMLREKAV QAAIVPVCLL ENMDQEGLIN KKDFIALLSR PTPLPCLTST PLYPDWSFAA
LPAVSDALAD RVTRALFNAP AAASFHWGAP ASTSQVEALL RDVRQHPQQR RLWLDVKSWL
IQHQLMVGGV ILAFLLLTLN YIWVMLLVRR RGKQLERNSV VLHQHERALE TARQMSVLGE
MTSGFAHELN QPLSAIRHYA QGCLIRLRAA DEQHPLLPAL EQIDQQAQRG ADTLRNLRHW
VSQAQGNPVL TEAWKAIAIR EAIDHVWQLL RMAQQFPTVT LHTEVSAALR VTLPSVLLEQ
VLANIILNAA QAGATHLWIV AERTENGISI VLQDNAGGID EALLRQAFQP FMTTRKEGMG
LGLAICQRLV RYGRGDISIR NQTAPDGLSG TVVTIHFLHE NGGRDGDNSS TG
