SENX3_MYCTO
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