ID E6W6F4_DESIS Unreviewed; 501 AA.
AC E6W6F4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Selin_2578 {ECO:0000313|EMBL:ADU67289.1};
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:ADU67289.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU67289.1, 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; ADU67289.1; -; Genomic_DNA.
DR RefSeq; WP_013507158.1; NC_014836.1.
DR AlphaFoldDB; E6W6F4; -.
DR STRING; 653733.Selin_2578; -.
DR KEGG; din:Selin_2578; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_0; -.
DR InParanoid; E6W6F4; -.
DR OrthoDB; 9805967at2; -.
DR Proteomes; UP000002572; Chromosome.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ADU67289.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000313|EMBL:ADU67289.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT DOMAIN 1..68
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 280..501
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 230..264
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 501 AA; 56808 MW; 5AFBC01F9AB9A113 CRC64;
MHESVLHNLM IGLFVLNKDR TVVFWNRWMA QFSGISGSAA LGKTLGDIFV EPVNGRFSLA
LEDALRGHSS LLSHSLNKAP LPLYASNQMR LSETRIQQQI CIAPIRDQQQ ELFVAVQVVD
VSAAEHRERL LRNSDRRLRT LIDALPDFVC FRDREDRWQE ANRSAVDLLE LPAGFRGKSD
QELFGEIPLP LRIQGNHESV TLQRPEGAIS FDVSRLPIDD QGELVIGRDV TNYKRVEAQL
RELNQNLEKR VREETDKRLN QQRLLVQTSK MAAMGEMIQA IAHQWKQPLN IIAFLMQNLR
DISRNSTLEP QALEDAIEKT LQQVSFMVGT VDDFKNFFDP DKQKVSFSLL KAVREVDAIL
GEQLRTSNIK VVYQDAEQAS AAKIIGYPNE FKQVILSLFN NAKDAFMERE GRAEVREPFT
IGVEIEPLNG NRYAVTIRDN AGGIPPHIMD KLFTPYFTTK QAGTGIGLSL CKTIIEDHFG
GSITPGNWER GAFFRIELRN P
//
