ID A0A0M6YGQ1_9RHOB Unreviewed; 688 AA.
AC A0A0M6YGQ1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_1 {ECO:0000313|EMBL:CTQ49532.1};
GN ORFNames=JDO7802_01546 {ECO:0000313|EMBL:CTQ49532.1};
OS Jannaschia donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ49532.1, ECO:0000313|Proteomes:UP000049222};
RN [1] {ECO:0000313|EMBL:CTQ49532.1, ECO:0000313|Proteomes:UP000049222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ49532.1,
RC ECO:0000313|Proteomes:UP000049222};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential protein that is involved in the control of cell
CC division, probably through the regulation of ctrA. Its phosphorylation
CC status is regulated by PdhS. {ECO:0000256|ARBA:ARBA00037447}.
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 -!- SUBUNIT: Interacts with DivL, PleC, DivJ and PdhS.
CC {ECO:0000256|ARBA:ARBA00038776}.
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DR EMBL; CXSU01000011; CTQ49532.1; -; Genomic_DNA.
DR RefSeq; WP_055084189.1; NZ_CXSU01000011.1.
DR AlphaFoldDB; A0A0M6YGQ1; -.
DR STRING; 420998.JDO7802_01546; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000049222; 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; -; 1.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; 1.
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; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CTQ49532.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000049222};
KW Transferase {ECO:0000313|EMBL:CTQ49532.1}.
FT DOMAIN 225..447
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 568..687
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 617
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 688 AA; 74400 MW; 3DA19CA99ABE6968 CRC64;
MDGSVPDTRY LEERRRRLAA ERRLDHSQRE LARAHSALVA NADRLSHRYL AQREQNLKLS
ARQDAVLKQR KEAADQADRA RRRLWHALEA MRDGFAVFDG QGHLVAANHV YLDLFDAASE
LAPGCHATEI FGLAAEEGAF DIGDLSPEEW AAEQVARWDL DVVPPLLLHH YDGRVVRFQD
RRGPDGDVVS LALDVTEQRD REIALSTARD EAEQMARAKT EFLARMSHEI RTPMNGVIGL
SQMLVEQSDD PEMTLYARTI RDSAEALLLI VNDTLDVSRL EAGKVDLRLA PMDMEALLID
CIRLAAATRH PNVQVGLSYP LDARTRFIGD EGRIRQIAMN LLGNALKFTE KGHVILRVSL
TDAGLDRTVA IMTVEDTGPG IPAAKAESIF EAFSQVDDPS KPTREGTGLG LTISRGLAER
MGGTLVLKQE QRASGGATFE LTLPLAQDGA APIRPALPPQ VTVPEGLGPR GDLAAERLVA
AGTRVVRTVS SDAAVVIVPL TLPPDAQPGL LNAIGPDARV ILLGRREEAC PALLVRAAAV
LPVPVAGSDL IAALAPPPVS KASPPQPRLL VADDNATNRF LVDRILRDQP FAVTMVDDGA
QAVAAFADAP PDAVILDISM PNVDGFEAAA AIRRIEAERG LRPVPLLALT AHLGDEMAPR
LKNAGFAAFL TKPLRKDVLL MALAEALT
//
