ID Q098H3_STIAD Unreviewed; 682 AA.
AC Q098H3;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STAUR_0289 {ECO:0000313|EMBL:ADO68098.1};
GN ORFNames=STIAU_2711 {ECO:0000313|EMBL:EAU68135.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU68135.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU68135.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU68135.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO68098.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO68098.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO68098.1; -; Genomic_DNA.
DR EMBL; AAMD01000021; EAU68135.1; -; Genomic_DNA.
DR RefSeq; WP_002612314.1; NZ_AAMD01000021.1.
DR STRING; 378806.STAUR_0289; -.
DR KEGG; sur:STAUR_0289; -.
DR PATRIC; fig|378806.16.peg.7445; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_76_7; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
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; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EAU68135.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EAU68135.1}.
FT DOMAIN 186..406
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 428..541
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 548..669
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 121..165
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 477
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 597
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 682 AA; 76413 MW; 11C3C787A68AE16D CRC64;
MTAAPFASRL LDALSREVAL VCEPSGLITW ADARAESILG ARKGTRLRLL AAQGTEEKVD
RLLLQAHEER VEGWELILCT SDHKPTTFAF RAQPYEGQVV MVGSLVPEDY GAALSQVSST
LSELSALHRE TERQQRELQR RADELQRLNR ELEESNRGVR SLHAALDEKA ESLQRAAEVK
GRVVANVSHE FRTPLHSILG LSKVLLNPLN GPLTSEQEKQ VQFVRTSAEA LYDLVNDLLD
LSKMEAGKAV LRPNRFVAGE FISALRGMMR PLLPPESSTE ILFPEIPSTV ELETDEAKLS
QVLRNLVSNA VKFTEKGSIA INVAQGPRDT VSFIVKDTGI GIPPEYHERI FEEFIQVETP
LHKKVKGTGL GLPLARRLTE MLGGTLTVQS VEGQGSTFTV TIPRVHPEVL EMAGLTERSQ
HLDPARAPVL VLEDDRQTLF LYEKYLERSG FQVVAVRSVE EARRAVQRMR PAAMVLDVML
EGETSWNFLA EMKSKEDTRD IPILVVTITD REQKARALGA DEFWLKPVEP HQLRRKLEEL
ANRGPVERLL IIDDDEVHRY LLKQVLKDTS YVLMEASGGR DGVQLAREKS PHLIFLDFLL
QDMTAFDVLD ELKADPRTRE IPVILHTSQE LKESERTRLA RETAAILAKH TLSREVAIAR
IRDALAKAGL GARFDEKEAR RG
//
