ID Q1D5B9_MYXXD Unreviewed; 700 AA.
AC Q1D5B9;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MXAN_3974 {ECO:0000313|EMBL:ABF87556.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF87556.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF87556.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP000113; ABF87556.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1D5B9; -.
DR STRING; 246197.MXAN_3974; -.
DR EnsemblBacteria; ABF87556; ABF87556; MXAN_3974.
DR KEGG; mxa:MXAN_3974; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_024627_0_0_7; -.
DR OrthoDB; 9805967at2; -.
DR Proteomes; UP000002402; Chromosome.
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 CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABF87556.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 326..363
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 464..684
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 700 AA; 76315 MW; 496CBBC1071284E7 CRC64;
MFGATEQSDW MKFLCLTSDD RHPVAEELRR QGQAVFITAD VVEAGAALGH GPVDVLVVDA
ADLVEDARWL DALRTRARPE EPLVLGLARE GTDAALEPLL AAGVDEFLVE PFTPVQVRSR
RLLLERRVAA RRQRRTSEAE ARGEVARLAS IIQMQSDVAM AGYGLDELMR LLCERSRVLC
GADGAAVALL GADTDEEVTY LVASGSLMPF IGFRLKVEGS LTGASLLQGE VMRTDDSETD
VRVNVTALRQ VGARSMICVP LWREGRPVGV LNVTSRRPNT FEDRDVRTLE LMAGLLGAAM
GNAAEAQARQ ELMVQNTLAM GALEESQELF ASFMDNIPAV AFMKDERGRR IWVNARYSRF
FGFPVGADMS NVSDVDLMPA ASAEQSRRDD DAVLTSGKQS ITEMMVPARD GTERHWLTYR
FIVRERSGRR LLAGVAVDIT DRKAMQAQLV VSDRLAAVGT LAAGVAHEIN NPLAFVLSNL
SFLAGELHAL APELPSGRMA ELEEVLREAT DGAHRVRQIV RDLRTFSRGD DEVATAVNVQ
AVLESAITLA RSELKLRAQL VRDYCEVPLV EGNEGRFGQV FLNLLINAAQ AIPMGQTEQH
EVRLSLRSAG DRVIIEVRDT GVGMPPEVRA RIFDPFFTTK PVGEGTGLGL SICHGIVTGF
GGDISVESEE GRGSTFRVSL PVARRAKEPV DPPLRMPLVG
//
