ID A0A0T6A0E6_9BACT Unreviewed; 669 AA.
AC A0A0T6A0E6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XU15_C0020G0038 {ECO:0000313|EMBL:KRT68536.1};
OS candidate division NC10 bacterium CSP1-5.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT68536.1, ECO:0000313|Proteomes:UP000051123};
RN [1] {ECO:0000313|EMBL:KRT68536.1, ECO:0000313|Proteomes:UP000051123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT68536.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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:KRT68536.1}.
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DR EMBL; LDXR01000020; KRT68536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6A0E6; -.
DR STRING; 1640516.XU15_C0020G0038; -.
DR PATRIC; fig|1640516.3.peg.2570; -.
DR Proteomes; UP000051123; Unassembled WGS sequence.
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 CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRT68536.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRT68536.1}.
FT DOMAIN 176..215
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 241..293
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 306..524
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 543..657
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 206..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 592
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 669 AA; 72873 MW; BCEDB02FD3095119 CRC64;
MPSHVTPRGN PDFEPVFGPV LEQIVGLLEA EAGVLWVWEE TAAAYVPALC RGRGSWAAPW
SPSHPEGIGR GDLDPSQETL LFDDLPPDSP LPAGEQKIRS FASVPIAVRA SGAGFLALYS
RRRGHFASRD LRFLQMVGEL MGRTIEQLGA AGGAQAGPTA GSIAEFRQVG DVSSMLIDAV
DVGVLVLDTE GRWSFGNRQI YEMLGYEPGE GPGRSGGPDP DAPPGFRASD LARLKRRDRA
CVFETRLFRK DGSTFTALVS STPRRGASEE SLGTIVLVTD ITERKQWDQQ VLRSEKLAAL
GTLAAGVAHN INNVLAAIVA RTDLLLRQVQ DRELKRWLNS IQQSALDGAS TVRRLQDFAR
TGAPESMVPV DLNGVITEVL QFTQARWKDE AELKGTRIDV VTELGDTPLI TGNPPELREV
FTNVILNALD AMPDGGCLIV RTCVEPGRDE GPWVEAVFED TGVGMTEEVR QKIFDPFFTT
KGVKGTGLGL STSYGIVARH RGSISVESEL GRGSRFCVAF PVPAELPRSP EDHARPVGRR
TGRILVIDDE PHLRDVITNL LRLEGHMAVG VGSGIEGVEA FRVEPFQVVI TDLGMPDLTG
LEVARKVREL NPEVKLILCT GWNAAVSQTE QEAVGIDRLL EKPFRLDKLL RLVHELLRTG
AQAEPRRQR
//
