ID A0A239FUR8_9RHOB Unreviewed; 737 AA.
AC A0A239FUR8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421757_102841 {ECO:0000313|EMBL:SNS60535.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS60535.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS60535.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS60535.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOY01000002; SNS60535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239FUR8; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000198426; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 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; 2.
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; IPR000700; PAS-assoc_C.
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; PF13426; PAS_9; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198426}.
FT DOMAIN 316..366
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 386..599
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 616..732
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 665
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 737 AA; 80737 MW; C79E9970EA9A37E6 CRC64;
MNQHPASSPA TVPSPDTVLL DAIEALSEGI AVFDSERRLV ISNERFAEML GPIRDMIVPG
LRWEDMLQAC VAGGIYADVS DRDREWRAKV GADGPQDVEI SQTDGCVYAI RYNATPSGGF
VIVRNDVTVS RQNKRLLEES EALLSNILGT NPTPVVMSRL RDGLILYRSP AARDLFGETV
NAVEHYENPS DREHYVRALR KEGKVDDFRM VFLGADRSRI PMSANGRLTQ YDGEACVVTA
LVDLRDSAAR EAIARKVVEN CPAPILMTDA ESGQVLFRSP EIDRIFGNKS NTKNFYIDPS
DREGFLDALR KDGLVLDYKA RFHRANGEPF WGAVSARMFD YEGRDVIVSY SRDLTEQIET
EATFSRRRER LFQNEKLSAL GGLLANVAHA LNNPLSVVSG NALMLEEESQ DPEVARKARR
IGEAAAKCTD IVRTYLTMAT KEDAALERSD INEIVGTALD VVRHELGEDG TVATADLAPE
LTQVLVDPDQ MAQVVINLLQ NAHAAISDAG KGSRIRVTTG AAPETGCIRL VVEDDGPGIS
EDIARKIFEP YFTTRGVGNG KGVGLTWCHS TLQAFDGQIH IDRTYRNGAR FVIDLPAVKA
TPEATQEDGE DETTARILVV DDEPDVADLN AEILQRVGYE VTIAYSGAEA IEAMEGTAFD
CILCDLNMPE TDGRAVYDHV RRCHPDSLSK IGIVTGDTMG RASQTFLLEA ARPYLEKPVS
PTELRDFVAG ILAGGGR
//
