ID E6W5U2_DESIS Unreviewed; 753 AA.
AC E6W5U2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Selin_2514 {ECO:0000313|EMBL:ADU67227.1};
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:ADU67227.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU67227.1, 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; ADU67227.1; -; Genomic_DNA.
DR RefSeq; WP_013507097.1; NC_014836.1.
DR AlphaFoldDB; E6W5U2; -.
DR STRING; 653733.Selin_2514; -.
DR KEGG; din:Selin_2514; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_71_0; -.
DR InParanoid; E6W5U2; -.
DR Proteomes; UP000002572; Chromosome.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT DOMAIN 136..208
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..265
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 262..334
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 336..388
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 389..445
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 462..513
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 531..746
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 753 AA; 85760 MW; 79825B98D110EBD9 CRC64;
MADTSKSPPH ILFLHAFHAS PFIQLLFRGN GELAEASDGA LRALRCQREK LPEHPWLRQT
DALQLNNAVK MVARTGEPAV TAIQLPQGEI FLELTQVSLT SQQTCWVLAT QTELTDTIAS
GSSPGLQKRK EELLANRQRW QFALEGTNIG VWDWNIQSSE VYFSPRWKEI LGYRDHELPN
SLEQWQQRIH PDDYQRVMQA HEPAFSKSDR LYRSEYRLRH RDGNYRWISS QGKVMSWARD
GTPLRMIGTH ADITERKILE EQQERMVRIL EATTDSVNIA TPDGTMIFWN SHGRAMVGVE
PDEDVTAISF DLFHPPKSLK ILTRVAIPSA ITNGIWQGEN VITNRHGKTI PVTQVIIAHR
DQQGNLEYLS SIMRDMSPQK KVEEALRSSE QRLWRLLEST PLGVVIINSC GTIEWVNPAM
CHKVHYHFES LAGHSLTKIL PEESRMAWHQ WFEQFGNAHT SSSEEWKFVR RGGESFLAEI
VSTSFADTSG QWRMVAYVTD ITKRKRFEDE LLRSLRQQEE LNELKSTFVQ MVSHEFRTPL
AGIMGSAELL KKYLERLSPE RRDEHLDTIL SGVQRMVFMM EEILALGAMD SGQTNFSPSP
VDLVAMCRAI QDQLHSIFPG QRIQLDFRDI PTCAMLDESL LHHILTNLLS NALKYSPATS
PVHFSIFNTT KELCFRVTDF GIGIPESDRG RLFEAFFRGS NASHIQGTGI GMMIVKRCLD
LHNGTIQIQS KPNQGSTFTV TIPLSQCIAE EKS
//
