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Database: UniProt
Entry: A0A142YI47_9PLAN
LinkDB: A0A142YI47_9PLAN
Original site: A0A142YI47_9PLAN 
ID   A0A142YI47_9PLAN        Unreviewed;       914 AA.
AC   A0A142YI47;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=luxQ_5 {ECO:0000313|EMBL:AMV38712.1};
GN   ORFNames=VT85_14835 {ECO:0000313|EMBL:AMV38712.1};
OS   Planctomyces sp. SH-PL62.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV38712.1, ECO:0000313|Proteomes:UP000076365};
RN   [1] {ECO:0000313|EMBL:AMV38712.1, ECO:0000313|Proteomes:UP000076365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV38712.1,
RC   ECO:0000313|Proteomes:UP000076365};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-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};
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DR   EMBL; CP011273; AMV38712.1; -; Genomic_DNA.
DR   RefSeq; WP_068416555.1; NZ_CP011273.1.
DR   AlphaFoldDB; A0A142YI47; -.
DR   STRING; 1636152.VT85_14835; -.
DR   KEGG; plh:VT85_14835; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000076365; Chromosome.
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; 1.
DR   CDD; cd17580; REC_2_DhkD-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; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 1.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AMV38712.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076365};
KW   Transferase {ECO:0000313|EMBL:AMV38712.1}.
FT   DOMAIN          17..87
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          138..209
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          485..537
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          555..773
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          795..911
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          528..555
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         844
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   914 AA;  101430 MW;  D32565D2013912B3 CRC64;
     MHKSESNDSA CASSKSQAAR FRSLFDNRLV GIDIVDAEGR WVEINDRLCE LLGRSREELT
     GRRLDEFTHH EDLEVEAALA RRLFNGEIRS YRLEKRFLRG DGGWARVEVD ALLVDDEPGP
     LRASVILDLG DRERDREESA RLQTLVEQSP LGVVVIDPET ARFLQFNETA HESLGYAREE
     FAGLTLADID EQKTHEAAVG RIAMVLKTGR ARFEASQWTR KGELRRVRVT ARRVFLDGRP
     CVQSVWQEVA ASRDSSTEQA RQDATIRQIL RTAPLPMGIA ELREDDGDIL HIFDNRAACR
     SFARPAGSTS GRWGGAELGM DGAALKAWIA AYRASQRLGR AVHFEDGRDF GGEQRWLRIV
     VSYVGPATSG RDRFCYIAED ITERKRAEAE ILRLNRSLER RAAELQTIFE VIPIGVGIAD
     DPECRSIRAN PALARILGTE VGVNVSLNAP ESERPTTFKA FHGGHEVAVD DLPMQVSAKR
     GIALHDVEID VAFEDGRVVN LLEHVSPLFD EQGSPRGCVA AILDVTEWRR AQRERERLLE
     DLREADRRKD EFLAMLAHEL RNPLSAAGNA AEILRLKEPD DPETRWCCEV IERQTRRLAR
     LLEDLLDVSR ITRGKIVLRR ETMDLRGAVE RAVETIRPMI EERRHQVEVH LPAEPLWVHA
     DPARIEQVVV NLLGNAAKYS EEGRSVSVTV SRNGESAVVR VEDQGIGMSP AVLEKVFEMF
     SQVESSIDRS RGGLGIGLTI ARSLVELHDG RISATSEGLG SGSTFLVRLP CVGDPAPDDP
     SPPRPANATR ATPRRIVVVD DNVEAVVALA RLLELAGHTV ATAFDGPSGL EAVDDFRPDV
     ILLDVGLPGM DGYQVAERLR SLPDGHALFL VALTGYGQES DRHRAFDAGF DRHLIKPVEV
     ETILEVIASA LPPS
//
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