ID A0A0W7WIW6_9RHOB Unreviewed; 842 AA.
AC A0A0W7WIW6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AVJ23_11635 {ECO:0000313|EMBL:KUF10525.1};
OS Pseudoponticoccus marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoponticoccus.
OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF10525.1, ECO:0000313|Proteomes:UP000054396};
RN [1] {ECO:0000313|EMBL:KUF10525.1, ECO:0000313|Proteomes:UP000054396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF10525.1,
RC ECO:0000313|Proteomes:UP000054396};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KUF10525.1}.
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DR EMBL; LPXO01000006; KUF10525.1; -; Genomic_DNA.
DR RefSeq; WP_058862364.1; NZ_LPXO01000006.1.
DR AlphaFoldDB; A0A0W7WIW6; -.
DR STRING; 1685382.AVJ23_11635; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000054396; 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; cd00130; PAS; 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 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; IPR000014; PAS.
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:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
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 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 Kinase {ECO:0000313|EMBL:KUF10525.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000054396};
KW Transferase {ECO:0000313|EMBL:KUF10525.1}.
FT DOMAIN 339..560
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 577..688
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 716..833
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 625
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 765
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 842 AA; 93679 MW; 290921D5AC752F53 CRC64;
MELADKLAEE RRARLAAERL LAQKQAELFE ANRKLGQHAL QLSHEIKETR SQVAVVRDEN
LRVRHQLGQA TQQIEVVTDQ LLKALQTIRD GFAMFDALGR LELANPAYLS VFDGLETIGP
GASYSHVLQM LVEEGIVNLQ GEAGPDWAAR MLARWQSDPI PDEVLRLWNG RFVKLQDRHL
PDGGVVSLGI DITELMRMWS AVEELPDGFV IFDAEDRLLM CNEPYRQLYS QSAPAMVPGA
SFEEILRYGL ERGQYADAIG REEEWLEKRL AQHRIPRTEL EQKLDDGRWV RVFERETSDG
GRAGLRIDIT QTKEDQARLK EAMIRAEAAN RAKSAFLANM SHEIRTPMNG VVGMADLMRE
TELTEEQALY VDTIRSSGEA LLVIINDILD YSKIEADKLQ LHPEPFDLER AVHEVVMLLQ
PSARDKDIAL LVDYDMFLPT RFVGDPGRIR QILTNLLGNA VKFTVDGHVM VRVTGVMERD
GGTSIHLTVE DTGIGIPADK VDHVFGEFNQ VEDERNRQFE GTGLGLTITR RLVELMGGEV
WVESEPGRGS CFGLRIQLPA DEPIKYESAQ LPEALKQVLV VDDHGANRQI LSKQLAILGL
QTAFCTTGAE ALDRMHPPPD VVLIDQDLPD MTGQDLVAQL RQAGAAIPVI LLCDNPGHLE
RRPGAEVQAV LQKPAPRRAL FDALEAVGPG LSPAVPDSAA PDAPDPQAAE EPARLDVLLA
EDNRTNQLVF RKMIKEFAIE LRVANNGIEA VEAFRDRRPD LIFMDISMPR MDGKQATREI
RRIEGDGPHV PIVAVTAHAM AGDREGVLTA GLDDYLTKPL RKAELAEKIT TYGGQRMAQM
AS
//
