ID Q0YQ87_9CHLB Unreviewed; 840 AA.
AC Q0YQ87;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CferDRAFT_0474 {ECO:0000313|EMBL:EAT58467.1};
OS Chlorobium ferrooxidans DSM 13031.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT58467.1, ECO:0000313|Proteomes:UP000004162};
RN [1] {ECO:0000313|EMBL:EAT58467.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58467.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT58467.1, ECO:0000313|Proteomes:UP000004162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58467.1,
RC ECO:0000313|Proteomes:UP000004162};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans DSM
RT 13031.";
RL Submitted (JUL-2006) 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:EAT58467.1}.
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; AASE01000019; EAT58467.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0YQ87; -.
DR OrthoDB; 9783713at2; -.
DR Proteomes; UP000004162; Unassembled WGS sequence.
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; 2.
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; 3.
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; 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; 2.
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; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
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; 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; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EAT58467.1};
KW Kinase {ECO:0000313|EMBL:EAT58467.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EAT58467.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004162};
KW Transferase {ECO:0000313|EMBL:EAT58467.1}.
FT DOMAIN 278..330
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 331..402
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 476..697
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 718..834
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 769
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 840 AA; 94656 MW; 9738C804E6B91A9E CRC64;
MFMNQKRPDS DTLSELCAKA EAGLRNSQDN AVEFSASPEE MRRLIHELTV HQLELNMQHE
ELFQSRIELE KSLNRYADLY DFAPVGYLTL SRESRIVEGN LTAAKILGVS RSLLPDKYLY
NFITAYDRTP FTAFIEQVFT LKGEPSYCEV SLKPKAVQAD QLHLATPSSV RMDAVLNDNG
ENCRLVLTDV TRQQKAEHVI SANHERQQLI LKETHSGIWE WDIKSNTNVW SDELWPMYGL
EQNDLEASYE LWKECIEPRE RSAVETAVWH AVQQGEDFSI EWRVRNCPDP GRWLMSKGIP
YKDQTGEITR YVGIVVDITE LKRARQIGIE ERLFTKNVIE SIPGAYYIID TNGSYIGWNA
FLRDEIVGKP ESEMLHTPVG SVLHPEDLPV VQQKIINVIE HGIEEKVEAR VLLRGGPEFR
WYLLTGKKII IDGNTCVIGT GIDITEQKQI EEENAQLEMQ LVQSQKMEML GTLAGGIAHD
FNNMLGVILG YTEMLLDEFS PADAHYLDID AIREAAARSA ELTQQLLAFA RKQTIVPEVF
QLNASVEKML PMLRRLIGEN ITLHFVPATN KTQIKIDPSQ IDQILVNLCV NARDSITGNG
QITIKINRCD IAESSSELSK KVVEYLALSV NDDGCGIAKN DIPHIFEPFF TTKEQGKGTG
LGLSTIYGIV KQNNGRIDCK SESGIGTTIT VYLPLNRDQS ASEREEVSDP LTHQGDHTIL
IVEDEPGILK LCKLMLERKG YRVLVAETPR DAITLADKYN EKIDLLLTDV IMPEMNGQDL
SEIILAVRPD IKILFMSGYT ADALGGTTNI HTEHHFIRKP FTITSLNNAV FDTLNADNPL
//
