ID A0A062XM27_9BACT Unreviewed; 854 AA.
AC A0A062XM27;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EG19_05325 {ECO:0000313|EMBL:KDA53622.1};
OS Thermoanaerobaculum aquaticum.
OC Bacteria; Acidobacteriota; Thermoanaerobaculia; Thermoanaerobaculales;
OC Thermoanaerobaculaceae; Thermoanaerobaculum.
OX NCBI_TaxID=1312852 {ECO:0000313|EMBL:KDA53622.1, ECO:0000313|Proteomes:UP000027284};
RN [1] {ECO:0000313|EMBL:KDA53622.1, ECO:0000313|Proteomes:UP000027284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP-01 {ECO:0000313|EMBL:KDA53622.1,
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:KDA53622.1}.
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DR EMBL; JMFG01000020; KDA53622.1; -; Genomic_DNA.
DR RefSeq; WP_053335110.1; NZ_JMFG01000020.1.
DR AlphaFoldDB; A0A062XM27; -.
DR STRING; 1312852.EG19_05325; -.
DR OrthoDB; 175518at2; -.
DR Proteomes; UP000027284; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; IPR000014; PAS.
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; PF01590; GAF; 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; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..285
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 509..714
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 737..851
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 196..225
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 786
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 854 AA; 92977 MW; AA60453C7FF79E4E CRC64;
MSDPRRQVAK PLVRLALTLQ LLLLVAGVVG YLQGSNYLEL NLRRSVEHSA AVAVNHWQRT
LELIYQQGQE VPQEPKAAHL MPVPSLDAAT LVKEATPPVK EMRPLPGVDE GFWLWWPGGF
GQGLSGLSVV KAQEGCRQCH PQFVPGEVVG GLSFRVETPF LSRILYARKL SLITLIGSLL
LLTSAAVWLM TGVALKRERQ AEKEREEAER QLAASEQLYR TLVDHSLVGV YLIQGDRFLY
CNPRMAEMFG YSQDEVIQQK LVADLVAPED RERVAENLRK RFTGEVQFVR YTFSAMKANG
TRFPVEVFGA RVVLPSGPAV LGTIVDNSEQ EAARQVVEAA YRAVVALPGE NVFQAAAESV
AALLHVPVVF VAEEIDGQLS LLGAHGAVQK ELIPLAGTPC EVAIREKRPL ELASGFAAQF
GTPGWIQVVP ECYFGMPLVG SAGQALGILA VLDSKPRQLS VLERQILEIY AVRLGRELER
LHLLRQQKEL ESRLAAHEKL AALGVLAGGI AHDFNNVLAG IVAEAEVLRR LVPPEAHEKV
EHLVSLAQRG GEVVRRILSF ARPSVTKPEP IAVAELVQDT VELAHHTFGP QFHFDLQVEG
ELFVLGEEAL LQQALLNLLT NARDAMPEGG SVAIRAYPRN GEVVLEVEDQ GTGIDPVHLP
RVFDPFFTTK PRGQGTGLGL TTVYRTVEAH GGTVAIDSRL GVGTKVTLTL PRIPPPQTTK
PSAAPSTLKA SRPAGCGVLL VDDEPAILEG LRQVLELEGY RVVCAKSAEE ALRSFQPSEI
HVAVVDVLLP GVNGIQLAQH LLEKKPDLAV VFSSGHTPEA LPPGLVSRDS VVFLQKPYTA
RVLLETVERL CSRA
//
