ID E3FHL5_STIAD Unreviewed; 984 AA.
AC E3FHL5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=STAUR_1283 {ECO:0000313|EMBL:ADO69087.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO69087.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO69087.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69087.1,
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; ADO69087.1; -; Genomic_DNA.
DR AlphaFoldDB; E3FHL5; -.
DR STRING; 378806.STAUR_1283; -.
DR KEGG; sur:STAUR_1283; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_301460_0_0_7; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 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; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..275
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..557
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 743..962
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 961..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..293
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 984 AA; 109508 MW; 2A562B772BE5E2AC CRC64;
MRRHEHLPPP HSKPMSLRRL AASAPGRYAI AVLSVGLALL LQKAAWPFMP TSPFLFFFLA
VMFSGWWGGW GPGLLSIGLA ALLADHFFLS PANSLSVTAG DGVALSLFTV LSLLMTRLNT
ALRQTSMERA VLLERERLAR ARAETEQARF HALLMQAPAI VALFQGADHV LTLSNPLSTA
LLGQRALLGK PLRESVPELA PQGFLALMDR VYSAGAPYTG QETSWSFLQA DGSTKTYVLD
LVLQPIRDVH GRIDGVACFA FDRSESVLAR QRMEELNTAL KRSKEQYQGF VSQSTEGIFR
LETHQPLPIA QPVQAQVDAI LEHGYIAECN DAMARMYGLE SAAALTGTRL GKLLVREDPH
NQESIKAFIR GGYRLEEAES HEATHDGRPR VFINNLVGVI EKEHLVSAWG TQRDVTEQRR
AEEALRHSEE RLRIAVNSAA IGTWDLNLVT GAYQCDERCR QLFGLSTAVS LRIDAIRSGV
YPEDLERFER ELARAFTPSS GGDFRIEYRT LGTEDGVARW VSVHGRAFFN EQARAVRFTG
TVLDVSERRR TEASTRFLAE ASAVLSSSLD YENTLSNVAR LTVPELADWC TVDLKPPGEP
FRRVAVATAV PEDAEFARQV KNIHLDLEKY SAHPSAQAFL RQQPVLIEQI HLERFLENAR
SDEHTRLIRT LQPLSFIAVP LVERGRAFGV LSFFSTRSGR RYTARDLTFL EELAHRMALS
VENARLYREA QEAIRLRDEF LSIASHELKT PLTPLSLKLQ MLSREVKRQP DSPLRRSVED
YIVIGTRQVK KLSELVSDLL DVTRIAGGRL RLEPEPVTLD LLIREVAARY EPEAARLGSR
LQLELQGSVE GHWDRLRLEQ VITNLVDNAI KYGAGKPIHV GLHTRENQAW LHVRDEGIGI
APQYLSSIFG RFERAVSERH YGGLGLGLYI TRTIVEAMGG SIHAESVLGE GATFTLALPL
TPGESAAQDS SEEPSEADSA TRDT
//
