ID A0A062XZ75_9BACT Unreviewed; 1019 AA.
AC A0A062XZ75;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EG19_10035 {ECO:0000313|EMBL:KDA54754.1};
OS Thermoanaerobaculum aquaticum.
OC Bacteria; Acidobacteriota; Thermoanaerobaculia; Thermoanaerobaculales;
OC Thermoanaerobaculaceae; Thermoanaerobaculum.
OX NCBI_TaxID=1312852 {ECO:0000313|EMBL:KDA54754.1, ECO:0000313|Proteomes:UP000027284};
RN [1] {ECO:0000313|EMBL:KDA54754.1, ECO:0000313|Proteomes:UP000027284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP-01 {ECO:0000313|EMBL:KDA54754.1,
RC ECO:0000313|Proteomes:UP000027284};
RA Stamps B.W., Losey N.A., Lawson P.A., Stevenson B.S.;
RT "The Genome Sequence of Thermoanaerobaculum aquaticum MP-01, The First
RT Cultivated Group 23 Acidobacterium.";
RL Submitted (APR-2014) 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:KDA54754.1}.
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DR EMBL; JMFG01000005; KDA54754.1; -; Genomic_DNA.
DR RefSeq; WP_053334775.1; NZ_JMFG01000005.1.
DR AlphaFoldDB; A0A062XZ75; -.
DR STRING; 1312852.EG19_10035; -.
DR OrthoDB; 9761183at2; -.
DR Proteomes; UP000027284; 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 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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
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; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027284}.
FT DOMAIN 134..205
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 208..260
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 261..311
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 334..386
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 464..517
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 594..644
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 657..880
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 899..1015
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 110..137
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 950
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1019 AA; 113958 MW; 2D34016C33DDC577 CRC64;
MGTQKLVAAV DVGDPAVDQQ VKAALEALGC EVVHEPGVAV DVVISDSPES SPSQQRDPED
AGPVRLPYRV HLLHEDEPLP QAMGASCDDV VRYCRNFEEF KLRLQARLRV VEQTRRLVKL
EQSLSQAMAK LQSSEERSRT LVESITDVFY VTDANGRLVY GSPNLFSYTG YQPRELLHRT
YLKLVAPEDR RWLVALYLAK TAEGASEVAC EFRALRKDGS RVWVDQRTTI VRDRQGRVVE
YRNVVRDISE RKAMEEALKE GEERYRSLYE NVAIGLYRTT PDGRILMANP ALVHMLGFET
FEELAQRNLE EEGFEPGYPR ALFRQRLESE GQIVGLESAW KRRDGSVIYV RESARAVKDE
SGRVLYYEGT AEDITERVTA EKALTESEER YRLISEMISD YAYAFRVEAD GTMRGDWLTE
SFTKVFGWTI EELDRRGGWV GAVYPPDLPL WVEHAGKVLH GQPDVTEGRF VTRDGEVRWL
RDYAVPIFDP AAGRVTRIVG ASQDITEKRK LEEALEASNE LFRALADAAP AAVLVLQGDR
LLYANKFAKN LVGFSDVERR NEENFDVLKL VDPAFREQVR SWGYARERGE PAPNRYELPI
RTRDGKRRWL DFSVVTFPYR GQPARMAVAV DITDKKATEE ALLHAQKMEA IGRLAGSVAH
DFNNMLLVIM AHAELLKLKA GQDPRFLAAV DGILGASTRA AELTRKLLAF ARKQQVHPER
LDLNHEVGGT LKVLKRLLGE NVELIWRPAE DLWPVVLDRS QVDQVVANLV VNARDAVGEK
GHIWVSTANR QLSEEDCRLL PEAKPGRYVV LAVKDDGCGM DSEVLKRIFE PFFTTKGEGK
GTGLGLATVF GIVKQHNGFI VVESEPGRGS TFEIYFPVVE GEKAEARDAA APIPRGWETI
LLVEDQPEVL EAASSLLKQL GYQVLSAKGP EQALAVAASY QGVIHLLLSD VGLPGMSGSE
LAQHLVAVRP EMKVLLMTGY TQEAPLRTEA EKAWGPVLEK PLTAEALAHS VRQVLEGKA
//
