TRCS_MYCTU
ID TRCS_MYCTU Reviewed; 509 AA.
AC P96368; F2GHA7; I6XAE7; P96908; Q79B74; Q7D8Z0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Sensor histidine kinase TrcS {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:10089160};
DE AltName: Full=Tuberculosis regulatory component sensor {ECO:0000303|PubMed:10089160};
GN Name=trcS {ECO:0000303|PubMed:10089160};
GN OrderedLocusNames=Rv1032c {ECO:0000312|EMBL:CCP43783.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND AUTOPHOSPHORYLATION.
RX PubMed=10089160; DOI=10.1006/mpat.1998.0265;
RA Haydel S.E., Dunlap N.E., Benjamin W.H. Jr.;
RT "In vitro evidence of two-component system phosphorylation between the
RT Mycobacterium tuberculosis TrcR/TrcS proteins.";
RL Microb. Pathog. 26:195-206(1999).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=11914351; DOI=10.1128/jb.184.8.2192-2203.2002;
RA Haydel S.E., Benjamin W.H. Jr., Dunlap N.E., Clark-Curtiss J.E.;
RT "Expression, autoregulation, and DNA binding properties of the
RT Mycobacterium tuberculosis TrcR response regulator.";
RL J. Bacteriol. 184:2192-2203(2002).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=Mt103;
RX PubMed=11953357; DOI=10.1128/iai.70.5.2256-2263.2002;
RA Ewann F., Jackson M., Pethe K., Cooper A., Mielcarek N., Ensergueix D.,
RA Gicquel B., Locht C., Supply P.;
RT "Transient requirement of the PrrA-PrrB two-component system for early
RT intracellular multiplication of Mycobacterium tuberculosis.";
RL Infect. Immun. 70:2256-2263(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT "Deletion of two-component regulatory systems increases the virulence of
RT Mycobacterium tuberculosis.";
RL Infect. Immun. 71:1134-1140(2003).
RN [6]
RP OVEREXPRESSION IN M.SMEGMATIS.
RX PubMed=31088763; DOI=10.1016/j.tube.2019.04.017;
RA Sarva K., Satsangi A.T., Plocinska R., Madiraju M., Rajagopalan M.;
RT "Two-component kinase TrcS complements Mycobacterium smegmatis mtrB kinase
RT mutant.";
RL Tuberculosis 116S:S107-S113(2019).
CC -!- FUNCTION: Member of the two-component regulatory system TrcS/TrcR
CC (PubMed:10089160, PubMed:11914351). Phosphorylates TrcR
CC (PubMed:10089160). The TrcR-TrcS regulatory system may act as a
CC transition regulatory system involved in adapting to an intracellular
CC environment and transitioning from latency to reactivation
CC (PubMed:11914351). {ECO:0000269|PubMed:10089160,
CC ECO:0000269|PubMed:11914351}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10089160};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:10089160};
CC Note=Can use Ca(2+), Mn(2+), and, to a lesser extent, Mg(2+).
CC {ECO:0000269|PubMed:10089160};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expressed in broth-grown cultures and after 18 hours of
CC M.tuberculosis growth in cultured human primary macrophages, but not
CC after longer periods of macrophage infection.
CC {ECO:0000269|PubMed:11914351}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10089160}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an increase in
CC virulence in mouse model of infection, with significantly shorter
CC survival times (PubMed:12595424). In strain Mt103, disruption of the
CC gene does not affect the intracellular multiplication capacity of the
CC mutants in mouse bone marrow-derived macrophages (PubMed:11953357).
CC {ECO:0000269|PubMed:11953357, ECO:0000269|PubMed:12595424}.
CC -!- MISCELLANEOUS: Overexpression in M.smegmatis mtrB background reverses
CC the mtrB mutant phenotype including the expression of the MtrA-regulon.
CC TrcS interacts with MtrA and is capable of phosphorylating MtrA in
CC vitro. These results suggest that under certain specific conditions in
CC vivo, TrcS could phosphorylate MtrA, independent of MtrB.
CC {ECO:0000269|PubMed:31088763}.
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DR EMBL; AL123456; CCP43783.1; -; Genomic_DNA.
DR RefSeq; NP_215548.1; NC_000962.3.
DR RefSeq; WP_003405324.1; NZ_NVQJ01000018.1.
DR AlphaFoldDB; P96368; -.
DR SMR; P96368; -.
DR STRING; 83332.Rv1032c; -.
DR PaxDb; P96368; -.
DR DNASU; 887790; -.
DR GeneID; 887790; -.
DR KEGG; mtu:Rv1032c; -.
DR PATRIC; fig|83332.111.peg.1146; -.
DR TubercuList; Rv1032c; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; NAWVHTP; -.
DR PhylomeDB; P96368; -.
DR PHI-base; PHI:3617; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cell membrane; Kinase; Manganese; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..509
FT /note="Sensor histidine kinase TrcS"
FT /id="PRO_0000451062"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 207..269
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 284..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 287
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 509 AA; 54591 MW; 8EA2F0B3DB565922 CRC64;
MIPDRNTRSR KAPCWRPRSL RQQLLLGVLA VVTVVLVAVG VVSVLSLSGY VTAMNDAELV
ESLHALNHSY TRYRDSAQTS TPTGNLPMSQ AVLEFTGQTP GNLIAVLHDG VVIGSAVFSE
DGARPAPPDV IRAIEAQVWD GGPPRVESLG SLGAYQVDSS AAGADRLFVG VSLSLANQII
ARKKVTTVAL VGAALVVTAA LTVWVVGYAL RPLRRVAATA AEVATMPLTD DDHQISVRVR
PGDTDPDNEV GIVGHTLNRL LDNVDGALAH RVDSDLRMRQ FITDASHELR TPLAAIQGYA
ELTRQDSSDL PPTTEYALAR IESEARRMTL LVDELLLLSR LSEGEDLETE DLDLTDLVIN
AVNDAAVAAP THRWVKNLPD EPVWVNGDHA RLHQLVSNLL TNAWVHTQPG VTVTIGITCH
RTGPNAPCVE LSVTDDGPDI DPEILPHLFD RFVRASKSRS NGSGHGLGLA IVSSIVKAHR
GSVTAESGNG QTVFRVRLPM IEQQIATTA
