ID E6W4A3_DESIS Unreviewed; 1097 AA.
AC E6W4A3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Selin_1142 {ECO:0000313|EMBL:ADU65877.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65877.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU65877.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002432; ADU65877.1; -; Genomic_DNA.
DR AlphaFoldDB; E6W4A3; -.
DR STRING; 653733.Selin_1142; -.
DR KEGG; din:Selin_1142; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_283666_0_0_0; -.
DR InParanoid; E6W4A3; -.
DR Proteomes; UP000002572; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 290..336
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 361..415
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 583..652
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 656..706
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 725..794
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 798..850
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 870..1095
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1097 AA; 123230 MW; 39B2F608D339ED26 CRC64;
MFVPLAGALA VAVVVTLFLL QLASVRTEQR VSQARSEGQE RIVQLREQLE DALFDSYHVM
HATAREVAEL SPWSEERFAA AGSRVLQAQD AISAIALVSR QELAAVYPPS LAQNVPCFTS
KSIHRLSQNS STSATLRGPL FPSPDEAQVC MAIPLSATAD ADAGILLAAI NLASMLEKAG
SVDFRLDGMF LGLSKALSPV AEGEFAGHER AFRDDAVTTR LRFHDAEWYF SMAPQGQWGP
QVYSWVWVIA LFSVAAGSLS WYLFHQLMRM HRSSQRLVPE MRSRRQAQQE VRRMSRALEN
SACSVLITDI DGLIEYANPK TCRVTGYSQA ELLGSNPRLF SAGETPAEVY DAMWSDLLSG
REWVGELLNR RKDGSLYWEH VAISPILNQS GRIMSYIAVK EDITRRRQVE ITLERERGVL
EAIAQARPSS EILRTICAII QEQIPHSRCS FMLLDASGKV LQGCIHTDLP TEYVDLIVSV
PVREASGSCG TAAYRRQPVI VSDIATDPFW SGPFRVMALK HGLNACWSWP VLSSTEEVLG
TFAIYCRDQR RPEPHEELMV MRFASIAAIA VEKEEWREKL LLSEQRYRSF MESLNDGVII
TQDGLLRYLN QSMAQMVGYG RESLTETPFM TYIHPDDQAL AMDYHRRRMM GQQAPSEYDV
RLLCHDGRVI TVRVNSSLIT WNNRPAALAT VTDMTRRHEA QEQIRQLNES LERRVTEELK
RRMETETLLE GVFENSSVGI VAIDGRGQVL RANATYCQML GYCPEELREV GLDSLHPDDR
LTVVEHFESL MDGSAAMCQI EIRYLTRDGG LLDVQIVASA LNDENGDPRA ILAMVKDISD
LKVAIRRQRI QEQLLIQQSK MAVMGEMIGA ITHQWKQPLN ALSIILQEAR EDYQLGILPP
PVFSEAVERS LNHIDFMSRT IDDFRDFFRP DKSRVLFDII EAVEEVEKLL QKQLHLHSVS
MLYEISSENQ AHRAIYTVAN EVKQIVLNIL NNAIDAIAAA RVQGLLHRND NGIIRVRLET
TPMERILLIE DNGGGIPDEI LPRIFKPYFT TKADKGTGIG LYLSRMIMEN SLGGSISVTN
TPSGACFRLA FPTLQKE
//
