ID   SENX3_MYCBO             Reviewed;         410 AA.
AC   P0A601; A0A1R3XW13; O07129; Q11155; X2BF71;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Sensor-like histidine kinase SenX3;
DE            EC=2.7.13.3;
GN   Name=senX3; OrderedLocusNames=BQ2027_MB0500;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCG / Pasteur;
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 BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; Y13627; CAA73954.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIT99095.1; -; Genomic_DNA.
DR   RefSeq; NP_854163.1; NC_002945.3.
DR   RefSeq; WP_003402390.1; NC_002945.4.
DR   AlphaFoldDB; P0A601; -.
DR   SMR; P0A601; -.
DR   GeneID; 45424451; -.
DR   PATRIC; fig|233413.5.peg.544; -.
DR   OMA; SEHARME; -.
DR   BRENDA; 2.7.13.3; 3494.
DR   Proteomes; UP000001419; 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_0000074877"
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"
FT   CONFLICT        109
FT                   /note="F -> S (in Ref. 1; CAA73954)"
FT                   /evidence="ECO:0000305"
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