GenomeNet

Database: UniProt
Entry: A0A0F7GCF6_9CHLR
LinkDB: A0A0F7GCF6_9CHLR
Original site: A0A0F7GCF6_9CHLR 
ID   A0A0F7GCF6_9CHLR        Unreviewed;       623 AA.
AC   A0A0F7GCF6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DGWBC_0067 {ECO:0000313|EMBL:AKG52759.1};
OS   Dehalogenimonas sp. WBC-2.
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX   NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG52759.1, ECO:0000313|Proteomes:UP000034106};
RN   [1] {ECO:0000313|EMBL:AKG52759.1, ECO:0000313|Proteomes:UP000034106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WBC-2 {ECO:0000313|EMBL:AKG52759.1,
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011392; AKG52759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7GCF6; -.
DR   STRING; 943347.DGWBC_0067; -.
DR   KEGG; dew:DGWBC_0067; -.
DR   PATRIC; fig|943347.4.peg.66; -.
DR   Proteomes; UP000034106; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16921; HATPase_FilI-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_1.
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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKG52759.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..373
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          406..619
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   623 AA;  68478 MW;  F7BF7FDC47DB981A CRC64;
     MKVEEATVDN RPPRTIRFGL GVRFISFVVL VALLSGGLGG LMLIEMNRDY LHRQILQTNL
     SQSELAAEFT DKYITAVHAH VEVFAHRPDV MQAVSENLPE QLQTTISEFV NVQTALENVG
     IYDIYGIQRV VSNSNVSALG RSFIDALWFK TALSTGLPYQ DLPTISIISG EPVILYAVPV
     VNGSGLVTGI LTGEISLKGL AEAIVNVDYG TDTSALVADL RGEGIIIADT NPQYVMRPLS
     DRFDQTVLSL TVGSSDSFEA SNKGETELIG FASVPNLPWS VLVSTPKGTA TAMVDVMMKN
     ASLLLAGIIL VSAIVGGFAI LSVSRPLVQM RNISAKIAAG DLTKRVEVSQ NSEIGDLGAA
     FNHMAQEIAE KESRLVEYAM DLEKRVEERT LELSRSNTDL EQFAYVASHD LQEPLRMVSS
     YMQLLEKRYG SKLESEAKEF MNYAVDGANR MKVIINDLLQ YSRVGTRGKS PEPVNMEKVL
     KIAIANLSLA IKEYGAIISH EELPVIQADE SQMVQVLQNL IGNAMKFHSD ARPEIHIGVV
     DKDSEWQFSV SDNGIGLDPK YADRIFIIFQ RLHTRDEYPG SGIGLAMSKR IIERHGGKIW
     VESTPGQGAT FYFTITKKEN ENE
//
DBGET integrated database retrieval system