ID Q1DFU4_MYXXD Unreviewed; 838 AA.
AC Q1DFU4;
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_0197 {ECO:0000313|EMBL:ABF90162.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90162.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF90162.1, 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; ABF90162.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1DFU4; -.
DR STRING; 246197.MXAN_0197; -.
DR EnsemblBacteria; ABF90162; ABF90162; MXAN_0197.
DR KEGG; mxa:MXAN_0197; -.
DR eggNOG; COG0697; Bacteria.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_339732_0_0_7; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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 PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABF90162.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..591
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 606..829
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 811..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 91077 MW; 1232468F1F4D0727 CRC64;
MSSSPSPQIQ ALPPPALLPL TWPAAVVGLM FGVLMTYVPY EFRVASFRPL YPYVRMLGLT
YLTGSIMLMG ALLYPRAPRW LDVTGRLLLG AAMALYWWVL NVLPGSFTGI ILYPVLFGGV
VLEAWPAMRQ RPVLRTFAAL TGAAFGVAML VVPERFPLSV YAHLAPLRPL VGLLFAVCGV
GLLLPSHWLH RRLPALFMGG LAVPFALLAY ALGRGASWLG ASVYAVLTLA CVAQALDWRP
RAPRTVGWKL LRGLAFAGLV PLLALGGLAA YLAQNAIEQQ VRDDTQRAAA GEADFLRRYL
DDAGESLALM LESPGFRAAF AAAAPERLEP YLVNLAAQER AFDAALAVDT QGHILAASPS
VEGWNLEPRD FLPPAFTRGA EVSPPFIRPP GQPLVAVTQP FREDGEVRGM LVGLLSLERL
SQATTPASRR FHVQVLDRRG LKVLRDTAPG APLLGEAHLP DALSLELLRP GIGVLEAFDA
ADRRILAAEA PVEGTEWNVL VTQELVVAYA AITRMSAAVV GLVLLGVLMA LLLSQLVARD
VIRRLDHLRS ATAALTAGDW SQRVDVEEDD ELGELARGFN EMAARTGATQ TELKEAVRAR
EEFLSVASHE LRTPLTPLKG FAALTLQRLE KSGDFPERER LLKALRSMAR QTERLTRLVD
DLLDTARIQG GRLELERKRL DLVPLLGEVL ERFELRTESG VTFELDVPAH PVEGDWDALR
LEQVLTNLVS NAVRYSPHGG AVRMSLEAAE THVLLSVRDE GIGIPPENVA DLFRPFARAS
NAQARHFGGL GLGLFICREI VERHGGAIWA ESPGPQRGSS FHVRLPRRAE PAASASAA
//
