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Database: UniProt
Entry: Q0YRP3_9CHLB
LinkDB: Q0YRP3_9CHLB
Original site: Q0YRP3_9CHLB 
ID   Q0YRP3_9CHLB            Unreviewed;       892 AA.
AC   Q0YRP3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, 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   ORFNames=CferDRAFT_0944 {ECO:0000313|EMBL:EAT58970.1};
OS   Chlorobium ferrooxidans DSM 13031.
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT58970.1, ECO:0000313|Proteomes:UP000004162};
RN   [1] {ECO:0000313|EMBL:EAT58970.1, ECO:0000313|Proteomes:UP000004162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58970.1,
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:EAT58970.1, ECO:0000313|Proteomes:UP000004162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58970.1,
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:EAT58970.1}.
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DR   EMBL; AASE01000009; EAT58970.1; -; Genomic_DNA.
DR   RefSeq; WP_006366372.1; NZ_AASE01000009.1.
DR   AlphaFoldDB; Q0YRP3; -.
DR   OrthoDB; 9808408at2; -.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 4.
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; IPR013656; PAS_4.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 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; 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; 3.
DR   SMART; SM00091; PAS; 4.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:EAT58970.1};
KW   Kinase {ECO:0000313|EMBL:EAT58970.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EAT58970.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004162};
KW   Transferase {ECO:0000313|EMBL:EAT58970.1}.
FT   DOMAIN          266..323
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          338..388
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          385..431
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          458..510
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          528..746
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          770..885
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         820
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   892 AA;  100115 MW;  4B90ED29A01C864F CRC64;
     MQNSTHKGEE KERNAQQRES TLNAVFDAVD EPAFIMDREG TILDANQAFA RVYHKEVPAC
     ININAYDFFP PELAATRRIK AEEVFCTGRR MIYEDEQEGH CYRNTLYPIA GLDGRTSQLY
     IVAQDITDLK RAERDAETTQ TLFGALKEAV PGAFYMLDAE WHYAAWNAYQ RDVVVGRPDA
     AMASFTAIDA IHPDDRSKVG EKMANIMKSG VEESDVVRVL IQGGPRFRWF QLSGKRVFIK
     EKPFLIGVGT DVTEHKMKED EALHNSEERL RKLFDEHSAV KLVLDPLTGN IIDANHAAAA
     FYGWSIDELC RKHIREVDTH PEEELKHLLE QDRVSEKNQF PFQHRRADGS LRDVEVFSSN
     INVGGRELLY AIVHDVTERR AAERELQKLS VAMQQSHAIV VITDLKGDIE YVNPAFTIAS
     GYSQEEVIGK NPRILQSGTM QQSVYEELWG TILAGGVWKG EMYNRRKNGE FYWESAVISP
     VLNEEGVITN FVAIKEDITE KKKLWSELIA AKEHAEESDR LKTAFLANIS HEIRTPMNGI
     VGLSEILKDP DLSKEEQSLY IDLIDQSCQR LLYLINDIID ISRIEAGKTN VKISRTPVNT
     TLRDLHAFFK PLAEQKGLRL SCTTGLSDSE SVIETDSTKL TQILTNLLQN ALKFTREGHI
     DFGYARNKNT LEFYVADSGI GISPDMQTKI FERFRQADNS LTRNYEGAGL GLSISQAYIE
     MLGGLISVKS TEGKGSEFIF TLPYNPAGFV ETDVQPAAVK PNHDSLPGMT ILIAEDDAVS
     SILLEKTLQA ESITIISAGN GLDAVELVKE HPEIRLVLMD IKMPVMNGFD ATRLIKQLRP
     GLPVIMQSAF TSESERGKAE DAGCNSFITK PVNKARLLEL IHAALNRQPD KQ
//
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