ID A0A3M0CQG0_9PROT Unreviewed; 728 AA.
AC A0A3M0CQG0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=BXY39_0268 {ECO:0000313|EMBL:RMB11784.1};
OS Eilatimonas milleporae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC Kordiimonadaceae; Eilatimonas.
OX NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB11784.1, ECO:0000313|Proteomes:UP000271227};
RN [1] {ECO:0000313|EMBL:RMB11784.1, ECO:0000313|Proteomes:UP000271227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB11784.1,
RC ECO:0000313|Proteomes:UP000271227};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) 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}.
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:RMB11784.1}.
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DR EMBL; REFR01000009; RMB11784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0CQG0; -.
DR InParanoid; A0A3M0CQG0; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000271227; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000271227};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..267
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 271..323
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 341..566
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 598..716
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 570..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 648
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 728 AA; 80421 MW; D930D53D529EFD99 CRC64;
MAEPPFRYRT RTIIPIVCVG AVLSTVLLCL VWPGHDLAVR VAAGLIASAA AVGLTLHSIR
AQAQKNIMPE TVLGLAQDML GIGYWYVDPA TNHVVWSQGV YAIHARDPSA PPPGMEEAIA
YYHPEDRMMV RRHLQRAVKE KAGFRFRLRL IADDGQEKHV LSIASFTKLN GRDLLYGVFQ
DVSDRVRREQ DLVTMQERFA MAQTSMPMGV FDYDIGRDEL VWDDAMFEIY GFSRQDFGGR
YEDFLGRLHP EDSEQANHRL QSALVDEAGL YNTRFRIVRD DGSQRWIKGC AVIQRDKNGL
PLRMVGLNVD VTDAADTEQR LQAALKAAEQ ASQAKSDFLA VISHELRTPL NGILGNLQLM
KRQTGSEDLL GLVDTAEHSG RLLLTHVSDL LDMAAIEADR MKLAPVSFNP AGLLDEAMAL
FQPLAEQKGL TLSLKTDPHM PPAIVADRHR LRQVIGCLVG NAIKFTEEGT VTVKADFNHF
RAATGSVGMT VKVTDTGIGI SQDDQRHLFT PFMAADNTLS RRHGGLGLGL SIAKYIAEAM
GGDLRCDSRP GEGSAFTFSV DVPVADHWTD SDGREETVRN GHANGHTNGT ETTIPRRSLL
VAEDVSVNQQ LLEKVLVARW GQDVTFVDNG EEAVNLLKER HFDAVLMDIQ MPVMDGVTAT
RKIRAEMPQH SGMPIIAVTA NALGEHVKEY LISGLDYCIT KPVDWTELQA LLQDLDSLAD
LTARRHQA
//
