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Database: UniProt
Entry: A0A2S8S477_9RHOB
LinkDB: A0A2S8S477_9RHOB
Original site: A0A2S8S477_9RHOB 
ID   A0A2S8S477_9RHOB        Unreviewed;       746 AA.
AC   A0A2S8S477;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LX70_03271 {ECO:0000313|EMBL:PQV55606.1};
OS   Defluviimonas denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Defluviimonas.
OX   NCBI_TaxID=404881 {ECO:0000313|EMBL:PQV55606.1, ECO:0000313|Proteomes:UP000238338};
RN   [1] {ECO:0000313|EMBL:PQV55606.1, ECO:0000313|Proteomes:UP000238338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18921 {ECO:0000313|EMBL:PQV55606.1,
RC   ECO:0000313|Proteomes:UP000238338};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (FEB-2018) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:PQV55606.1}.
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DR   EMBL; PVEP01000008; PQV55606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8S477; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000238338; Unassembled WGS sequence.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 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; 2.
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; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000238338}.
FT   DOMAIN          239..459
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          477..585
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          609..728
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          24..97
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         658
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   746 AA;  82573 MW;  D058FAF1C379D7F9 CRC64;
     MVTAIVSEVR VNFVDRLAKE RRGRLAAERL LEQKQRELFA ANAQLARHAQ SLTAQIREQR
     DGLESARHEA EALRGQRSQA LSELERATAA AQIAERRLWE ALETIRDGFA LFDEKQRLIA
     ANGVYLSMIG AGEELPRGLG YADVIASLAE RALPEADPDM RRDWQSRMIA RIDGEEIEPE
     VLDLADGRHF RLMDRRGAFG DLVSLARDIT QAVAREGELR EARERAEAAS RAKSAFLANM
     SHEIRTPMNG VVGMAELLCE TDLTEDQRLC AETIRTSGEA LLTIINDLLD YSKIEAEKLK
     LYPEPFDLER CLHEVMLILQ HTAQDKGVAL LADYDMFLPT RFIGDRGRVR QILTNLLGNA
     VKFTARGHVL ARVVGIEREE AFELHISVED TGIGIAAENL EAIFGEFNQV DSQSNRQFEG
     TGLGLSITRQ LVDMMGGQIW VDSELGHGSC FGFQIMLPAA EPGLAPSRDR RPILLKRALV
     IADVQIDRTI LQRQLQTFGI EVTACRRIED AVETLDATDV DLILAEPAEA SAAGDLVRAI
     RARDGTVPVA FVLPDDAELH EGPGLYRLTR PVLRNALFDL IEVLSYPGLA LPVPVEEAPP
     PVPVARRMRV LAAEDNRTNQ LVFRKMVEDL DIDLVFAVNG REAVDLWQSF RPDLIFMDIS
     MPGMDGCEAA EAIRAAEAAQ NRRRVAIVAL TAHARESDSE AIMAAGLDRF LTKPLKKAEI
     LSAVDAFAPE GVLPPRRAEG QPSARI
//
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