ID A0A1W1UGP2_9DEIO Unreviewed; 1650 AA.
AC A0A1W1UGP2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN00790413_05443 {ECO:0000313|EMBL:SMB80192.1};
OS Deinococcus hopiensis KR-140.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=695939 {ECO:0000313|EMBL:SMB80192.1, ECO:0000313|Proteomes:UP000192582};
RN [1] {ECO:0000313|EMBL:SMB80192.1, ECO:0000313|Proteomes:UP000192582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KR-140 {ECO:0000313|EMBL:SMB80192.1,
RC ECO:0000313|Proteomes:UP000192582};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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};
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DR EMBL; FWWU01000004; SMB80192.1; -; Genomic_DNA.
DR STRING; 695939.SAMN00790413_05443; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000192582; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 6.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 4.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 6.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 7.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SMB80192.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000192582};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 98..155
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 195..247
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 287..339
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 379..431
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 471..523
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 563..615
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 655..707
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 952..1185
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1263..1376
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1385..1501
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1531..1648
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 880..942
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1312
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1434
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1581
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1650 AA; 177473 MW; 211888AF61EE09E8 CRC64;
MTETALVDAL DDQLLLSALL AFRDGDFSAR LPSNWTGVAG KIADTFNEVL VSTGRVAQDV
ARVGHIVGKE GKVTQRIPLG RAVGGWAELI EGVNTLVDDL VWPTSEMTRV ITAVANGDLS
QTMALEVEGQ PMQGQFLQTA RTVNTMVSQL NSFAGEVTRV AREVGTEGKL GGQADVRGVG
GTWKDLTDNV NFMAGNLTNQ VRNIADVTTA VANGDLSKKI TVDARGEILD LKNTINTMVD
QLNSFAGEVT RVAREVGTEG KLGGQADVRG VGGTWKDLTD NVNFMAGNLT NQVRNIADVT
TAVANGDLSK KITVDARGEI LDLKNTINTM VDQLNSFAGE VTRVAREVGT EGKLGGQADV
RGVGGTWKDL TDNVNFMAGN LTSQVRNIAF VTTAVANGDL SKKITADARG EILELKETIN
TMVDQLNSFA GEVTRVAREV GTEGKLGGQA DVRGVGGTWK DLTDSVNFMA GNLTSQVRNI
AFVTTAVANG DLSKKITVDV RGELLELKDT INTMVDQLNS FAGEVTRVAR EVGTEGKLGG
QADVRGVGGT WKDLTDNVNF MASNLTDQVR GIAQVVTSVA NGDLKRKLTL EAKGEIAELA
ETINSMIDTL ATFADQVTGV AREVGVEGRL GGQASVPGAS GTWKDLTDNV NRLAANLTTQ
VRAIAEVATA VTKGDLTRSI NLDARGELDA LKDNINAMIH NLRDTTEKNE EQDWLKTNLA
RFTRMLQGQR DLLTVSRLIL SELAPLVKAS HGVFYTMDED APTPTLQLQA SYAYRERKGL
GNRFLLGEGL VGQCALEQQP IVLTHVPHDY VQINSGLGAA TPTSIIVLPV VFEQQTKAVV
ELASFSTFSP THIAFLEQLT ESIGIVLNTI QATMRTETLL AQSQGMAQEL QSQQEELRQT
NEELEEKARL LAEQNREVER KNHEVESARQ ALEEKAAQLA LTSKYKSEFL ANMSHELRTP
LNSLLLLANQ LRENPEGNLS AQQQNYAKTI YASGNDLLNL INDILDLSKV ESGTVTADVA
DVPYRVVGEA LEATFAPVAA DKGVGFELRF DSSLPASLAT DEKRLLQILK NLLANAFKFT
SRGSVTLEVA PAVGGWSLDN TSLLRAPGVV AFRVTDTGIG IPADKQRVIF EAFQQADGST
SRKYGGTGLG LAISRELARI LGGEITLEST PGSGSVFTLY LPAGRRGMDF TPAAGGARNM
VVGLNTTSSM GWTGLDTPSA SSVGGASSLA PISPVPAAEG TAAPLPSAHV GDDRAVIQPG
DRTVLIVEDD PTYAGILLEL AHERGFLGLI ATRGDQAITL AQTYRPTAVT LDLSLPDTSG
WAVLDHLKHD PATRHIPVHI ISGEEATLTG RKLGALDHVT KSGDKAALTR AFANLESFIA
RRVKNLLVIE DDPAQRENIV ELIGNGDVKT TAVSSGAEAL AALEATPFDC IVLDLQLTDM
TGFELIQALQ KNPAYKSIPV IVYTAQDLTR QQETQLRKAA KSIILKDVRS PERLLDEVTL
FLHRVEANLP EAKRQILEGA RQQDPTLQGR RVLVVDDDIR NIFALTAVLE RHRMTVYTAE
NGRDAISMLE STPDIDAVLM DVMMPELDGY ETTRLIRQNR KFKSLPIISL TAKAMPGDRE
KSIESGASDY ISKPVNTDQL LSLLRVWLSR
//
