ID A0A0F7GCA9_9CHLR Unreviewed; 702 AA.
AC A0A0F7GCA9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DGWBC_0023 {ECO:0000313|EMBL:AKG52716.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG52716.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG52716.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG52716.1,
RC ECO:0000313|Proteomes:UP000034106};
RX PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA Molenda O., Quaile A.T., Edwards E.A.;
RT "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT Dichloroethene Reductive Dehalogenase, TdrA.";
RL Appl. Environ. Microbiol. 82:40-50(2015).
RN [2] {ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA Molenda O., Edwards E.A.;
RT "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT in Dehalogenimonas sp. WBC-2.";
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};
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DR EMBL; CP011392; AKG52716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7GCA9; -.
DR STRING; 943347.DGWBC_0023; -.
DR KEGG; dew:DGWBC_0023; -.
DR Proteomes; UP000034106; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
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; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..702
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002515707"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..564
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 587..699
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 637
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 702 AA; 78580 MW; C03A8E8A4B396DE0 CRC64;
MPLPIHRLIM GCLASILFLC AGALPAHAQT PSIRVGIYQN HPQVFWEEDG KPQGIFIEVL
DSIAKAESWN IEYVPLIFSD GLDMLETGAI DILVSVGVNA DRQQLFDFNS INIISNWARI
YLPKGSGVTS ILDLNGRTIA AVRDDIHYSA FQKQTQLFGI NCVFEELDSY DAVFAALTDG
TAEAGIVNRL VALRLAPEYD VIPSDIIFNP IEIRFAFTKG RHTELISTID AYLAEMKADP
DSIYHQALMR WIESPVVEKS VIQPWVFWVM GITLLILGLF ILTSARLRIS IRRRTSELAA
KRREYAYERK LRHRTEEERE KIQAALIQSQ KMEAVGQLAG GVAHDFNNLL TGILGYAEMT
LYDLDDKEQI KENITEVIHA GERAAKLTQQ LMVFSRRHET QDEIICLNDV ITGVEKLLRH
IVRANINFNF LPGEGILEIR GDHNQLEQVM MNLAVNASDA MPDGGNLTIK TENIYLDEDH
YLMNADFKPG NYVCFSMEDT GIGMNKETIA HIFEPFFSTK PEGKGTGLGL AVVYGVVKSH
HGFVNVYSEP DKGTVFRIYL PVSEEDAGTC TDNPPKMQPD PSGKNEKILV VDDDRLVNDF
ASRVLRSRDY IVYTAESLAT AQETLKRHAD IDLIVSDVVL PDGTGMDLVH NLRPGTRVIL
SSAYVGSLNN RDKIAGSGYH YLQKPYSISD LLQAVRRMID DT
//
