SENX3_MYCTU
ID SENX3_MYCTU Reviewed; 410 AA.
AC P9WGK5; L0T5I7; O07129; P0A600; Q11155;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Sensor-like histidine kinase SenX3;
DE EC=2.7.13.3;
GN Name=senX3; OrderedLocusNames=Rv0490; ORFNames=MTCY20G9.16;
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 [GENOMIC DNA].
RC STRAIN=2296207;
RX PubMed=9426136; DOI=10.1046/j.1365-2958.1997.6361999.x;
RA Supply P., Magdalena J., Himpens S., Locht C.;
RT "Identification of novel intergenic repetitive units in a mycobacterial
RT two-component system operon.";
RL Mol. Microbiol. 26:991-1003(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Probably forms part of a two-component regulatory system
CC SenX3/RegX3. Phosphorylates RegX3 (Probable). {ECO:0000305}.
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 membrane; Multi-pass membrane protein.
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DR EMBL; Y13628; CAA73957.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43224.1; -; Genomic_DNA.
DR PIR; E70744; E70744.
DR RefSeq; NP_215004.1; NC_000962.3.
DR RefSeq; WP_003402390.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P9WGK5; -.
DR SMR; P9WGK5; -.
DR STRING; 83332.Rv0490; -.
DR PaxDb; P9WGK5; -.
DR DNASU; 887185; -.
DR GeneID; 45424451; -.
DR GeneID; 887185; -.
DR KEGG; mtu:Rv0490; -.
DR PATRIC; fig|83332.111.peg.538; -.
DR TubercuList; Rv0490; -.
DR eggNOG; COG5002; Bacteria.
DR OMA; SEHARME; -.
DR PhylomeDB; P9WGK5; -.
DR BRENDA; 2.7.13.3; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:1990748; P:cellular detoxification; IMP:MTBBASE.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
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 membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..410
FT /note="Sensor-like histidine kinase SenX3"
FT /id="PRO_0000074876"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 164..380
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 385..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 410 AA; 44825 MW; 3C215149FD843206 CRC64;
MTVFSALLLA GVLSALALAV GGAVGMRLTS RVVEQRQRVA TEWSGITVSQ MLQCIVTLMP
LGAAVVDTHR DVVYLNERAK ELGLVRDRQL DDQAWRAARQ ALGGEDVEFD LSPRKRSATG
RSGLSVHGHA RLLSEEDRRF AVVFVHDQSD YARMEAARRD FVANVSHELK TPVGAMALLA
EALLASADDS ETVRRFAEKV LIEANRLGDM VAELIELSRL QGAERLPNMT DVDVDTIVSE
AISRHKVAAD NADIEVRTDA PSNLRVLGDQ TLLVTALANL VSNAIAYSPR GSLVSISRRR
RGANIEIAVT DRGIGIAPED QERVFERFFR GDKARSRATG GSGLGLAIVK HVAANHDGTI
RVWSKPGTGS TFTLALPALI EAYHDDERPE QAREPELRSN RSQREEELSR
