ID Q09CZ9_STIAD Unreviewed; 729 AA.
AC Q09CZ9;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STAUR_0106 {ECO:0000313|EMBL:ADO67915.1};
GN ORFNames=STIAU_2903 {ECO:0000313|EMBL:EAU69624.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU69624.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU69624.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU69624.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO67915.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO67915.1,
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; ADO67915.1; -; Genomic_DNA.
DR EMBL; AAMD01000004; EAU69624.1; -; Genomic_DNA.
DR STRING; 378806.STAUR_0106; -.
DR KEGG; sur:STAUR_0106; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 5487456at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAU69624.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 218..290
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..346
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 359..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 599..715
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 648
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 729 AA; 81465 MW; B79BC5906DF5F782 CRC64;
MIHRQDFSLE HRVPNEPSTV SRVPLERALP AALLSTVSED RKAVPLSHPE QLRLENLRSY
EILDTPPEPS FNDIAYMAAL LCGTPTAFIS LTDETRQWFK ASTGVNEALE VPRDDSFCTY
AIQQKELFVV PDAALDARFR DNPYVAGGPR IRFYAAAPLV TQEGFVLGTV CAIDRMPREL
TPQQGRSLEA LAGQVVSLLE LRRMNLHQQR LIDELRTTNE RLEMIQHATN DIIWDWDLVT
GRVVWNSRIT DVLGYTLEQV GEHSDWWYRH IHPDEQERLA QSFQRALAEG APKWTAEYSL
RRSNGTWARV LDRSTIQRDA AGKPVRIYGA VVDLSEREEM RTRLALTDRM ASVGTLAAGV
AHEINNPLAY VIANLDFTLQ EVATAGTPGG TPVEELSQAL EEAREGAERM RVIVRDLKMF
SRPDDERMEL VDLCHAIDSA ATMAWNEIRH RARLVKAYQS VPPLYANEAR LGQVFLNLLV
NAAHSIPEGA ADRNEIHVST RLDAAGRIVA EVRDTGSGIP EEIRPRILEP FFTTKPSGVG
TGLGLSICHG IINSLGGTLE FESEVGRGTV FRVVLSPPER PESMPLPGEP APQASRRGRI
LVVDDEPMVL TALKRTLDEE HDVILFNGAR AALEWLEQGQ PWDLILCDLM MPEITGMDFH
EELSRRMPER AGHVIFVTGG AFTARARDFL GRVSNPRTEK PFDARALREL VNARLNLAGP
ASGPSYKRH
//
