ID A9WK17_CHLAA Unreviewed; 537 AA.
AC A9WK17;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Caur_1239 {ECO:0000313|EMBL:ABY34468.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY34468.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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}.
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DR EMBL; CP000909; ABY34468.1; -; Genomic_DNA.
DR RefSeq; WP_012257124.1; NC_010175.1.
DR RefSeq; YP_001634857.1; NC_010175.1.
DR AlphaFoldDB; A9WK17; -.
DR STRING; 324602.Caur_1239; -.
DR EnsemblBacteria; ABY34468; ABY34468; Caur_1239.
DR KEGG; cau:Caur_1239; -.
DR PATRIC; fig|324602.8.peg.1423; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR HOGENOM; CLU_000445_114_15_0; -.
DR InParanoid; A9WK17; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 3.30.450.20; PAS domain; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABY34468.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW Transferase {ECO:0000313|EMBL:ABY34468.1}.
FT DOMAIN 69..124
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 163..384
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 419..535
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 122..149
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 468
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 537 AA; 59508 MW; 2C519B61BB29F5A0 CRC64;
MSLSVEQRVL IETGSAYVVV DPDLRIQSAG GMLALLGGKP PIGGHLLDLL PELFGNEAAL
DEILHGERDR LYLPLINRQM PDGSTLYIDL LTIPLTDKDG RITGLIQIVT DTTQRSVIEQ
LRSQQRNELQ LLKDRLQRQN VELARINASL LKTTKIKDEF LASMSHEIRT PLTAILGMVD
LLRAQLVGPL SDEQMGAIDG IKKGSQHLLS LINDYLDIAK VEAGRMELDL TPVSVQDVCM
SLRPLVADLI RRANLSLIFD IDSAVQVILA DARRLRQILI NLLSNAIKFT PAGGKVGLEV
RGEPERGAVR FTVWDTGIGI SAEDAVRLFE PFQQIESERQ KEVTGSGLGL ALVAKLVRLH
GGSVRVESEV GVGSRFHVTL PWEPDEQYRF LEQLDQQERE EDTHPTELPA ASPRAGDRPL
LMVEDDVASA TLIADYLRRC GYRVVHVESG EEALAYIQGE LPCLILLDVR LRTMSGFEVM
QHLRSQVATR DLPVLVLTAL AMPGDRERCL EAGADEYLAK PIRLRLLAER IAALLER
//
