ID Q1D948_MYXXD Unreviewed; 970 AA. AC Q1D948; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=MXAN_2606 {ECO:0000313|EMBL:ABF90438.1}; OS Myxococcus xanthus (strain DK1622). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90438.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF90438.1, 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}; CC -!- INTERACTION: CC Q1D948; Q1D8M1: MXAN_2785; NbExp=3; IntAct=EBI-1574166, EBI-1574080; CC Q1D948; Q1D1W0: MXAN_5211; NbExp=3; IntAct=EBI-1574166, EBI-1574283; CC Q1D948; Q1CWQ1: MXAN_7059; NbExp=3; IntAct=EBI-1574166, EBI-1574240; CC Q1D948; Q1CWA4: MXAN_7206; NbExp=3; IntAct=EBI-1574166, EBI-1574045; CC Q1D948; Q1D8M8: phoP2; NbExp=3; IntAct=EBI-1574166, EBI-1574250; CC Q1D948; Q1CYI5: phoR3; NbExp=3; IntAct=EBI-1574166, EBI-1574436; CC Q1D948; Q1DDJ8: sdeK; NbExp=3; IntAct=EBI-1574166, EBI-1574809; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000113; ABF90438.1; -; Genomic_DNA. DR RefSeq; WP_011552676.1; NC_008095.1. DR AlphaFoldDB; Q1D948; -. DR SMR; Q1D948; -. DR IntAct; Q1D948; 38. DR STRING; 246197.MXAN_2606; -. DR EnsemblBacteria; ABF90438; ABF90438; MXAN_2606. DR GeneID; 41359983; -. DR KEGG; mxa:MXAN_2606; -. DR eggNOG; COG4191; Bacteria. DR eggNOG; COG5002; Bacteria. DR HOGENOM; CLU_310328_0_0_7; -. DR OrthoDB; 5477177at2; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd17574; REC_OmpR; 1. DR Gene3D; 1.10.287.130; -; 2. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2. DR InterPro; IPR011006; CheY-like_superfamily. 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; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1. DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1. DR Pfam; PF02518; HATPase_c; 2. DR Pfam; PF00512; HisKA; 2. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 2. DR SMART; SM00388; HisKA; 2. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2. DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1. DR PROSITE; PS50109; HIS_KIN; 2. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABF90438.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002402}; KW Transferase {ECO:0000313|EMBL:ABF90438.1}. FT DOMAIN 326..542 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 599..714 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 738..948 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT REGION 570..600 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 257..316 FT /evidence="ECO:0000256|SAM:Coils" FT MOD_RES 647 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 970 AA; 106705 MW; D3AFD8D044A58B91 CRC64; MTVPAELASA PSAPDTPELS VRMLRSVMLY YERTYGRDRL VRVWQREELP LTLAYVETLT NFVSVGFTER LFDVLDKDSG DPDFMTKAGR SIASPEAVGF LYYMMKALAT PRSVYERALE LDHTYNRVGG FHIDTLTDSR VQVRYVSRIR ERDRNFCRAR QGNLSAFPAI WNLPLAEVKE LRCQVDGADC CEYDIRWQSL PPLAWRYIVG GMAGMVAGLV SGTLNLAPPV FAVSSLGMVG VAAGAWLDTR AALLRKDEKL SEQHQGLQTS LEDLQRRNDE IFAANKALED RVAERTQELS EANTKLEASL ARQQELDRLK SEFFDNVSHE LRTPLTLILL TLEALAKEAE SLPPELPPLV TNMERSAQRL LRLINNLLDL AQLESGKARL RYQPLELFGF LSTVVPPFHT MAERQGVTLR LEGATVTPVH VDHERIEIVF QNLLGNALKF TQKGGVTVRV REDDSEVHVE VEDSGQGIAP QDIPVIFDRF SQADNSGTRR FGGSGIGLAL VKETLELHAG GISVTSELGQ GSVFHVRLPK GTAHIREDLR ERRQAVMPVR RERRISGAFP SLEPTGTDVL GASPPPARDH AGPGPESPRI MVVEDDPEIR SFLARLLAQH YRVMEAINGD DGRQRALRER PDLILSDVMM PVMSGLQMLT ALRNDPQTVD IPVILLTARQ EVTAKVEGLG TGANDYLGKP FSPNELLARI ETQLRLREAA VRAAENERLA AIGLLTSGFA HEVRNPLNGL MNALLPLKDM LTGGSADVEL SKAMLEVVEE CGQRIRHLAE SLLSFTRTSE SPVVLSLDSS LDSTLSVLAW KVPPGVKVER AYHCSEPIRG NPGALNQVWL NLLDNALRAV GDKGRVRIST ANTAEEAIVT IGDDGVGIRP EDMERLFQPF FSTRAAGEGT GLGLALSRRI IIQHGGSIAL SSVPGEGTQV EVRLPLRPVA PRVTGGLPDL ASEPRVGRLG //