ID K9ZYR6_DEIPD Unreviewed; 803 AA.
AC K9ZYR6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Deipe_0299 {ECO:0000313|EMBL:AFZ65900.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ65900.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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; CP003382; AFZ65900.1; -; Genomic_DNA.
DR RefSeq; WP_015234211.1; NC_019793.1.
DR AlphaFoldDB; K9ZYR6; -.
DR STRING; 937777.Deipe_0299; -.
DR KEGG; dpd:Deipe_0299; -.
DR PATRIC; fig|937777.3.peg.307; -.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_41_0; -.
DR OrthoDB; 9813394at2; -.
DR Proteomes; UP000010467; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13188; PAS_8; 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; 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; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ65900.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW Transferase {ECO:0000313|EMBL:AFZ65900.1}.
FT DOMAIN 203..255
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 256..328
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 589..803
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 552..586
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 803 AA; 90657 MW; F13995BD517FED38 CRC64;
MRDLLLSEAG VLYDALPGPL CITDARGNIL FINRAWRAAL NGGKATRPNL AITDLFHPED
QVTWQHHWEQ AALSGGFTGR FQVWQAEGRS CWYQLQVCRA AGREGERGSW LVSACDVDEQ
VRREHDLRRE VSELQGMVDA SAECIKLLDL DARLLSMNQG GMQVMEVEDF DACRNLLWSS
FWQGEVGVTI EHALQEARAG RTFTFEGQAA TMKGTLKWWE VRVSPIYDQQ GRIYRLLAIS
RDISLRKDAE KTRQESEMRL RSLIEASPIS ITTTSAGGTV TEANPATLAL TGWTPEDLKA
ERASWHRQTL PEYADLDRSA TEQALRAGRS EPYEKEILGA GGVRVPVRVV LARGEASEPQ
RFIWYIQDLR PQKAAERALS ELNTELECRV HQRTAELEER TVALDAFARF TDAVGTETDV
LALARGALSV IQARFVDATG VYYERKGETW QARVWTSDLA EDTRKVITQG IPVDAPVFAE
PLRRRSPWFV DHWNARREGI DHTEQYHAAA NLPLLLNNEV RGFLAVGLRH TGTWSDTDRA
MVQAIARGLN LALERTEHAR QLELQRRELQ EQTRELQGAN EELEAFAYSV SHDLRAPVRH
IAGYTALIHK SLGERLDPKT ARYLSVVDQS ATRMNTLIDA MLDLARTSRV PLRMESVDLD
ALVSRVRREL APDHESRSVQ WNVSPLPQVH GDQGTLYQVM VNLISNALKY SRTREVSRID
VWSEEHEHGW AIFVRDNGVG FDPRYGDKLF GVFQRLHRQE EFEGTGVGLA NVRRIVHRHG
GQVWAEGRPG EGATIGFTLS RTS
//
