ID Q1DEL2_MYXXD Unreviewed; 569 AA.
AC Q1DEL2;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MXAN_0643 {ECO:0000313|EMBL:ABF85915.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF85915.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF85915.1, 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; ABF85915.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1DEL2; -.
DR STRING; 246197.MXAN_0643; -.
DR EnsemblBacteria; ABF85915; ABF85915; MXAN_0643.
DR KEGG; mxa:MXAN_0643; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_025061_0_0_7; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABF85915.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000313|EMBL:ABF85915.1}.
FT DOMAIN 58..129
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 266..319
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 337..553
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 303..330
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 569 AA; 63084 MW; 128B0A5B20726844 CRC64;
MASARRPSTL TARAVPPIPT CMERDTPSAF RVEAFRAPMS RDAGNDDQRV SEESMASGID
ELSAWLDAAV DPFVACDAGE NVCFLNAAAE RLLGWTREEL IGQPASRLFP QRLHRHEGVS
LLRHLLSRRA ALGGRATRVL ARRKDGAEIM VELTVGASGK GRDERIVLNF RRLHEVVDTL
AEPVERTLHG LESESVPGDA LFRTVVEHAP MGIIYFDRSA IVIACNELFV SIIGSPKRLL
VGLNLLSLRD EGILHCVRET LAGHTCEYEG EYRAITSGRK TPVHVRFAPC FNAAGQVEGG
IGIVEDISER RRAERERERL YREAQEAIRV RDDFLSIASH ELKTPLTPLS LRLATLERRL
ARGELVESST LRQARLYLLR ITSLINDLLD SSRIEAGRLA LHREATRLEG LVEHVLHELE
PQRGNHTVRF DAPEQPVQVN VDPFRMEQVL ANLVENAFKY SPNGGTVRVS LRQRGGLALL
SVSDEGIGIP PDQQKLLFDR YFRARNASAH SFGGLGLGLY ISRDIVERHG GRIWVESEPG
HGSTFHVALP LMAGAPAQPN VEEPGQLIH
//
