ID A0A0L6CZX2_9RHOB Unreviewed; 721 AA.
AC A0A0L6CZX2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_1 {ECO:0000313|EMBL:KNX43256.1};
GN ORFNames=ROTO_00450 {ECO:0000313|EMBL:KNX43256.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX43256.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-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};
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:KNX43256.1}.
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DR EMBL; LGVV01000001; KNX43256.1; -; Genomic_DNA.
DR RefSeq; WP_050661017.1; NZ_LGVV01000001.1.
DR AlphaFoldDB; A0A0L6CZX2; -.
DR STRING; 74031.SAMN04488077_106206; -.
DR PATRIC; fig|74031.6.peg.45; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000037046; 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; cd00156; REC; 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:KNX43256.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW Transferase {ECO:0000313|EMBL:KNX43256.1}.
FT DOMAIN 222..444
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 461..573
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 587..704
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 7..59
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 509
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 636
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 721 AA; 79313 MW; 1BD4DB6493D581B9 CRC64;
MSLANKLAEE RRARLAAERL LEQKQAELHA ANRKLGKHAR ALSHEIHETR AEVQTVRDEN
LRVKSDLSEA HQKVEIAERR LWHSIATIQD GFAFFDADSQ MIAANHAYLA VFDGLEAVQP
GISYVEILQF ITEEGIVNIG AHAPHIWREH MLDRWQQATP EPEVIRLWNG HYIKLIDQRG
PDGDVVSLAL NITDTIRYET ELKEARRRAE TANRAKSTFL ANMSHEIRTP MNGVVGMADL
LMDSDLTEEQ RLYASTIKHS GEALLVIIND VLDYSKIEAE KLVLHTAPFD LERCIHELVT
LMQANARDKG LDLLVDYDLF LPTRFIGDTG RIRQILTNLL GNAIKFTETG HVLIRVTGVP
PAADEAAMIN VSIEDTGIGI PPDKVDHIFG EFNQVEDDRN RKFEGTGLGL AISQKLIRMM
QGDIWVESTP GEGSSFGISL TLPLAAPEDA ADPVLPRSAA RALIVEPQAA SRDILERQLA
ALGLDVVSCA SGAEALTLAC PEIDIVLCDH NMAGMDGLEL AEALRAAGHT IPIALLSQNT
GYAEQDPGRA HVQVVLQKPA PRRVLIDTLA VLLPSDQTMP KAARTMRVLA AEDNKTNRLV
FSKMLTSLDI ELQFAENGRE AVELFHSFRP DVIFMDISMP EMDGKEATRT IREAEDPGAH
VPIVAMTAHA MQGDEADILA AGLDHYLTKP LRKADIIARI TAACPPDARA PQPAPTTAQA
G
//