ID   SENX3_MYCTO             Reviewed;         410 AA.
AC   P9WGK4; L0T5I7; O07129; P0A600; Q11155;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Sensor-like histidine kinase senX3;
DE            EC=2.7.13.3;
GN   Name=senX3; OrderedLocusNames=MT0509;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Probably forms part of a two-component regulatory system
CC       SenX3/RegX3. Phosphorylates RegX3 (By similarity). {ECO:0000250}.
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 {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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DR   EMBL; AE000516; AAK44732.1; -; Genomic_DNA.
DR   PIR; E70744; E70744.
DR   RefSeq; WP_003402390.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGK4; -.
DR   SMR; P9WGK4; -.
DR   EnsemblBacteria; AAK44732; AAK44732; MT0509.
DR   GeneID; 45424451; -.
DR   KEGG; mtc:MT0509; -.
DR   PATRIC; fig|83331.31.peg.539; -.
DR   HOGENOM; CLU_000445_89_2_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..410
FT                   /note="Sensor-like histidine kinase senX3"
FT                   /id="PRO_0000428346"
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