ID A0A1U7P2W0_9DEIO Unreviewed; 804 AA.
AC A0A1U7P2W0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BOO71_0002614 {ECO:0000313|EMBL:OLV19499.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV19499.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV19499.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV19499.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLV19499.1}.
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DR EMBL; MSTI01000029; OLV19499.1; -; Genomic_DNA.
DR RefSeq; WP_075830774.1; NZ_MSTI01000029.1.
DR AlphaFoldDB; A0A1U7P2W0; -.
DR STRING; 249408.BOO71_0002614; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000186607; Unassembled WGS sequence.
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; 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; IPR013656; PAS_4.
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; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 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; PF08448; PAS_4; 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; 2.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 127..178
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 255..326
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 407..452
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 478..531
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 549..776
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 771..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 86530 MW; 5F6794681F8A36EA CRC64;
MNTATGSSAD AAAPFSGVDA AALLSALPDP TVWVRAGGEF ALNAAARERL GAVEGQAQNW
TALFLPDAAQ ALRDATALAL RGTSSRLSVT MPGAVAPALA TVTPAGPGAA LLHFRESHDP
LEVALDIMDR MGLGMTVQGA DTQILHANAS AAAILGLSPD QLTGRDSLDP RWRAIHPNGK
SFPGETHPAI VALKTGQPLL DVPMGVYHPA AEQWRWLKVT AIPRRAPGLD RPEQVTTVFA
DVTVQRHTSE ELSRSEQRFR SLVEATAQIV FTTDKLGNFS GPQPDWQAFT GQDAEQALNP
AVAIEAIHPE DRDQTMRGWA EALKSGQPHD IEHRLRRKDG VYVPMQIRAV PLRSADGSVR
EWIGAYTDVS AMRGAEVALK ALNAELEGRV AVRTQELAEV TRFSTLLLTA AGEGVFGLDA
SGRTTFANPA AGRLLGYSVE RLIGSQQHTL IHHSRADGTP YPPEDCPVHQ TLRDGQTRRL
DHDVLWHAQG HAVPVASVVT PLFSAAGTVT GAVLMVQDIT ERLRAQSQLQ EAIEDLERSN
TDLEQFAYVA SHDLQEPLRT LGSYAELLGR RYEGQLDDRA DRYLGFMQDA VGRMRGLIQD
LLEFSRVGRG ESVPTPLNLD DAMRAAADSV GAALHSNVDG EEGEQGEASL SWDTPDAVLA
HAPLIAPLLT NLIGNGLKFT APGQPVRVRV ESRQDGEMVH ITVQDNGIGI ALEYQERVFD
IFQRLHRRED YAGNGMGLAI CRKIVEHHGG TLWLESTPLP APDHGTTFHF TLPAAAPPSE
SHPPDSDSHP SDAGPAPTTD PHHA
//
