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Database: UniProt
Entry: A0A365TYL1_9RHOB
LinkDB: A0A365TYL1_9RHOB
Original site: A0A365TYL1_9RHOB 
ID   A0A365TYL1_9RHOB        Unreviewed;       755 AA.
AC   A0A365TYL1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-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=DQW77_08045 {ECO:0000313|EMBL:RBI73936.1};
OS   Roseovarius sp. TE539.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=2249812 {ECO:0000313|EMBL:RBI73936.1, ECO:0000313|Proteomes:UP000252940};
RN   [1] {ECO:0000313|EMBL:RBI73936.1, ECO:0000313|Proteomes:UP000252940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TE539 {ECO:0000313|EMBL:RBI73936.1,
RC   ECO:0000313|Proteomes:UP000252940};
RA   Liu B.-T., Du Z.-J.;
RT   "Roseovarius sp. strain TE539.";
RL   Submitted (JUL-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:RBI73936.1}.
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DR   EMBL; QNGB01000010; RBI73936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365TYL1; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000252940; 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   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; 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:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:RBI73936.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000252940};
KW   Transferase {ECO:0000313|EMBL:RBI73936.1}.
FT   DOMAIN          222..444
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          461..576
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          618..736
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          579..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..80
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         667
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   755 AA;  82655 MW;  DF958135AD701094 CRC64;
     MSLANKLAEE RRARLAAERL LELKKEELHA ANRKLGRHAR ALSDEIVETR AQVATVRDEN
     RKVKSDLTVA NEKVEIAERR LWLSIETIHD GFAFFDMDSR MIGANDAYLA VFDGLEAVKP
     GISYAEILQI ITEEGIVDIG AETPSAWRER MLDRWQSPDP EPHVIRLWSG EYIKLIDQRG
     HDGDLVSLAL NISDTVRYQK ELKAARHRAE AANRAKSTFL ANMSHEIRTP MNGVVGMAEL
     LAETGLSEEQ RLYTNTIRSS GEALLVIIND VLDYSKIEAD KLMLKPEPFD LERCLHELIM
     LMQPKARDQG LDLLLDYDIF LPTRLVGDPG RLRQVLTNLV GNAVKFTERG HVLIRVVGQT
     PDETGRTELH VTVEDTGIGI PPDKIGHVFG EFNQVDDAQS RKFEGTGLGL AISRQLIRLM
     GGEIWADSEP GRGATFGFRI ALPEAEGGVA AEPRLPVDLK QVMVVDPGAI GRGILERQLS
     QVGLSVATCK NGMAALDRLA GQDPAPDLVI CEHSMPGMDG LEFAEAAHAA GHAVPIILMS
     DNTGYAESDP ARRHLHTVLQ KPVPRQDLFA ALCVPEEHHA APPDAAPAEQ GNPAQAPQQP
     EATRQTAPDA AAPPRAMRIL AAEDNRTNRL VFSRMIKNLD IELRFAENGA EAVTLYREFD
     PDIVFMDISM PGKDGKEATG EIRAIEADTG VHVTVVAMTA HAMDGDSEGI LAAGLDHYLT
     KPLNKGAIIE RIAAARPEGA RDPEGGSADH CERTG
//
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