ID A0A3D9BW77_9RHOB Unreviewed; 769 AA.
AC A0A3D9BW77;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DRV84_05835 {ECO:0000313|EMBL:REC57692.1};
OS Rhodosalinus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57692.1, ECO:0000313|Proteomes:UP000257131};
RN [1] {ECO:0000313|EMBL:REC57692.1, ECO:0000313|Proteomes:UP000257131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57692.1,
RC ECO:0000313|Proteomes:UP000257131};
RX PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT saltern.";
RL Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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}.
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:REC57692.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QOHR01000005; REC57692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9BW77; -.
DR Proteomes; UP000257131; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 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; IPR036641; HPT_dom_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; 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; PF13188; PAS_8; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:REC57692.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000257131};
KW Transferase {ECO:0000313|EMBL:REC57692.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..160
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 265..485
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 515..631
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 769 AA; 77703 MW; C014DA8AFA94A72F CRC64;
MGQAVARPCA SSFRQSEPVM PWKTGASGRN RRAAPLVCAL ALAVAGGAAL ASAPVRDGRA
VLHDASRAAI AAPRAVPSRS RAPATAVVAA SMAAPLVLAG VVGLGGLLAA ATRWGVPRRS
GRTRRSEEAL AQLVDAAPDG IVVTDSQGRV LRANPAAAAL APALRPVAAH GEGAPRGAVA
LDDLLEDRIA PMIGAGAVRS RMRDGATGRR RVALTVTPIE GAGGERLLAV FLRAGDAEVE
GEPVPPARHQ PGGGDPPARE QAVAAVSHEM RTPLHALLAA LDLLPEAATA ADRDHLFAMA
RGSGARLRAM VEDALLFTRL SDAPGDAPVI APSGIARDAI AAQASRAAAQ RTDLRFEITG
EATPRHYRGC ASALARVVSG LVGQAVAAAP GGTVTVALHH GARAADGRTV LTLEVADDGP
PNARVAHEQV FAPFGDADRR VPYDGEDGLG LVVARAIVAA LGGTVTAERP PDGGARFRAT
LPLVEAEADA DPGARPASPA APSARPARAL PAGGAALVAD DAPVNVALMR RMVEQLGFTV
DTAADGATAA EMADRRSYAL AVLDYRMPGL TGVEVAQRMR ASERSGAAVI LCVSAVADLL
PPDALADAAV DAMLSKPLDG AALAAALEEV TSGAPLAAPD ALDAELDGVT NTLDRAELDA
LLGPDVAAKM IAAALAEAER ACAALGDTAL EREARVDIVH RAAGAAAMIG LGRLGALFRH
AQRELEAGHD AALPRVQALV QADLAEIAAA GVGDGEAGGT RKTAKDSES
//
