ID A0A2T4JIJ2_9RHOB Unreviewed; 742 AA.
AC A0A2T4JIJ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C5F46_08135 {ECO:0000313|EMBL:PTE17683.1};
OS Phaeovulum veldkampii DSM 11550.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Phaeovulum.
OX NCBI_TaxID=1185920 {ECO:0000313|EMBL:PTE17683.1, ECO:0000313|Proteomes:UP000241899};
RN [1] {ECO:0000313|EMBL:PTE17683.1, ECO:0000313|Proteomes:UP000241899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11550 {ECO:0000313|EMBL:PTE17683.1,
RC ECO:0000313|Proteomes:UP000241899};
RA Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA Chintalapati V.R.;
RT "Rhodobacter veldkampii.";
RL Submitted (MAR-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: 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:PTE17683.1}.
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DR EMBL; PZKF01000015; PTE17683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4JIJ2; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000241899; 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; 2.
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:PTE17683.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000241899};
KW Transferase {ECO:0000313|EMBL:PTE17683.1}.
FT DOMAIN 231..454
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 470..584
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 599..717
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 722..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..75
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 520
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 648
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 742 AA; 81992 MW; 90FB963C331D9D9D CRC64;
MHNSLAEKLA QERRARLAAE RLLDQKKREL FAANQKLALH ARALSEQIVQ QRHGLERARS
EAESLTAENS RVRFDLERAN SAALIAQRRL WEALETIRDG FAVFDADLRL VAANQAFLSV
FAGEIAVSAG VAYDAVLRVM ACHGMVELDG RDPLDWHHDM IARIRRPRIE PYVLRLASGR
HIRLIDRWGS EGDLVCLAQD ITPTIRREAE LEQARASAEA ASRAKSAFLA NMSHEIRTPM
NGVVGMAELL CETGLDEDQR LYAETIKSSG EALLTIINDV LDYSKIEAER LRLYPEIFDL
ERCIHEVMLL LQPKAHDAGI RLLVDYDLFL PTRFVADPGR MRQVLTNLLG NAVKFTPQGH
VLVRVVGLER GDGQVELHVT VEDTGIGIAP EHRDHVFDEF NQIETEGARI VQGTGLGLAI
TRHLVTLMGG SLWLDSEPGR GSCFGFRVVL PVAEPRDPAD LAPAQITLKT ALVVDDLMLN
RVILERQLQT YGLAVTLCRS GAEAVQVLGQ GARFDVLLTD HRMPEMDGLQ LTRRLRAMAL
DLPVLLLTSD PEAAAIETMR PALSGLLRKP VLRSDLFRAL QALSNREPAA ALAPLRQMRV
LAAEDNRTNQ LLLQQMLRGC DIDLHFATNG REAVDLWRKQ RPDLVFMDIS MPEMDGREAT
LAIRADEAAT GGHTPIVALT AHASEDDGAD LLAAGLDHYL TKPLRKGSII AQVRAHCPPE
ARAPLPQAAQ AEASAPADVR VD
//
