ID Q096S0_STIAD Unreviewed; 752 AA.
AC Q096S0;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STAUR_0751 {ECO:0000313|EMBL:ADO68555.1};
GN ORFNames=STIAU_0454 {ECO:0000313|EMBL:EAU67716.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU67716.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU67716.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU67716.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO68555.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO68555.1,
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; ADO68555.1; -; Genomic_DNA.
DR EMBL; AAMD01000028; EAU67716.1; -; Genomic_DNA.
DR STRING; 378806.STAUR_0751; -.
DR KEGG; sur:STAUR_0751; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_63_7; -.
DR OrthoDB; 5481157at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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; 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 PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 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; 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 Kinase {ECO:0000313|EMBL:EAU67716.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EAU67716.1}.
FT DOMAIN 392..462
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 531..751
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 82357 MW; A25B8D641D85B5C9 CRC64;
MSPAPPGEDT PVPRSWTDRH GRRPLKASGG LGPGSLALAA PVSSGVEDTI VHHAQCSGAR
ANRPLRLEGA MFEQEPARDT SGKERDEPLR LAAFLRDHHQ HILARWQNTT HALHSHRSAQ
GTPPVHHIPS LLEGITEALA HTEHGVPIQL PCILSDMHAF ARLDQGFDIH ELASEYGLLR
RCILQQLAAA ALRPSPSALA LLEELLDQSL SRAMLSYTRL RERTMNALDG MMQAAMDSPD
METLLHRLLC LLMETSLQVD SATILLCEGD GLQVRAALGL GAEKSLGLRL RGGKSFAGRI
AAGRQPMAVR PALEGVQDED ARRLGLLALY GVPLQEGGKL VGVAHMGSRT THAFSEADTL
LFRTMASRAT SLIIQAQLRA RELAARETAQ RSLAMLDGLL DSSTMGIAIL DRQLCFTRIN
EVLAKLNGAS VQEHLGCAFR DRVNPFIATS LEPLIRKVLE TGEPIEHFEL STPIGSEYLP
GHTWLISLFP VRASTGELLG VGDVVVDITV RKEAERALEQ AVSFREQLLA VLGHDLRNPL
SAINASAYQL SRQKSLDARG RQAVERIRRS GARMGRMIDD ILDFTRSRLG GGIPVTCQPM
NMGEVCRNAL DELQATFPQR QLLLEVQGDT SGSWDPDRVS QVLGNLVFNA LQHGSEETPV
RTVIRDEGAH VRMEVWNQGE PIPPEQLPHL FDPFKRRPSD QRPHEGRGGK RSLGLGLHIV
RQLAQAHGGE VEAHSSAEKG TCFEVRWPHN RA
//
