ID A9WF27_CHLAA Unreviewed; 1031 AA.
AC A9WF27;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Caur_2130 {ECO:0000313|EMBL:ABY35342.1};
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:ABY35342.1, 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};
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DR EMBL; CP000909; ABY35342.1; -; Genomic_DNA.
DR RefSeq; WP_012257996.1; NC_010175.1.
DR RefSeq; YP_001635731.1; NC_010175.1.
DR AlphaFoldDB; A9WF27; -.
DR STRING; 324602.Caur_2130; -.
DR EnsemblBacteria; ABY35342; ABY35342; Caur_2130.
DR KEGG; cau:Caur_2130; -.
DR PATRIC; fig|324602.8.peg.2412; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_0; -.
DR InParanoid; A9WF27; -.
DR Proteomes; UP000002008; Chromosome.
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; 3.
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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; 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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 118..189
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 243..315
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 319..372
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 538..610
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 613..665
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 678..900
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 919..1029
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 968
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1031 AA; 115425 MW; BA29E691E99DC6B3 CRC64;
MADARTHLIL FAIDDLREPI AQTLAPFPFI SYSFATTLPE LLDVINQHHS AIVLCRAEDY
VNMPVGLAII ILCVDDDLLF AHFANQPAIV DVLFENRLQR LPFIVQREIR QQQALDRETR
RLRMIIEHAP HGVIEVETSN RLIRWTNPAM NQLFGYSAAE MRSLRLEEMH PDEERATAID
TFHRMVAGDE SPILNVICQR RDGSIFYCNI APGGVYGNGQ RLIFIFFTDV TDEYQSLQTL
RVNAYRLELA LRAANQGLYD IDVRSGLTIV SDEYATMLGY DPATFTETNQ RWRERLHPAD
AAMVYQTYLD YLAGRIPEYR VEFRSRMQQG GWKWILSVGA IVERDAQGHP LRMLGTHTDI
SALKRLEFQE RLRVQLFTSL LGGESLENLM NILLKAFEEE QPDTRCALVL FDTTSRRQTH
VIASNLPSGL NDLLEEGLRQ PSQSRWQAIL ARQRLWIPDL RLDPQWTYYA ASAQHHGFTT
LWAEPISGAG GTIIGAFTVW SARNTLPQRD DQILLQFVGH LAGPVIEQHM IAERLRLSEE
RYTLAERAVQ DGVWDWDIIN GVTYLSPQWK ALFGFGEDEL PNAITTFFER IHPDDWPEVT
KALDRHFAGY EPFHMEFRMR YRDGKYRWVL ARGEALRDNE GTVTRMVGAL SDVTERRQLD
ERIRETQKLE ALGLLTGGLA HDFNNLLGII IGNLDLSLSD WQGDEATRQA IDSALQAALR
GAELTKSLLA VARRQPLAPT SIDVLQVIRE FLPLIQVTVG SAIKVQLIEQ ATSPARADRA
GLEAAILNLV INSRDAMPQG GSLTIKIREQ HVTSEDTMLL AILAPGCYIA IDVTDTGMGM
TPEVAERAFE PFFTTKERGR GTGLGLAMVY GFARQSGGTA QIYSTSGLGT TIRLYLPCTQ
GIVPEVVSPV PLAARREARI LVVDDDADLL QITATTLHNL GYTVFTATAS KAALTILQDE
AIDLLLTDVV MPEMDGLMLA AAAQQISPSL KVLYMSGFAA LQGTDMSNLA VIEKPFRAST
LEVAVQQALN A
//
