ID A0A2V2LLD4_9RHOB Unreviewed; 541 AA.
AC A0A2V2LLD4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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=DKT77_02970 {ECO:0000313|EMBL:PWR04026.1};
OS Meridianimarinicoccus roseus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meridianimarinicoccus.
OX NCBI_TaxID=2072018 {ECO:0000313|EMBL:PWR04026.1, ECO:0000313|Proteomes:UP000245680};
RN [1] {ECO:0000313|EMBL:PWR04026.1, ECO:0000313|Proteomes:UP000245680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TG-679 {ECO:0000313|EMBL:PWR04026.1,
RC ECO:0000313|Proteomes:UP000245680};
RA Ren Y.;
RT "Rhodobacteraceae gen. nov., sp. nov. isolated from sea water.";
RL Submitted (MAY-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:PWR04026.1}.
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DR EMBL; QGKU01000012; PWR04026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2LLD4; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000245680; 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; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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); 1.
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:UP000245680}.
FT DOMAIN 87..139
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 157..378
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 412..527
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 377..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 461
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 541 AA; 58533 MW; E4A8BF195250B437 CRC64;
MKPEHLDSWL NAPDDAFEAF FEQAPVYMFS ASADWTITRA SKAWCEGSGH ALDDLRGRCA
LEFLAPESRE KAETETLPRF TETRVIEGVQ LDFLRADGSV LPVVLSARAQ IDDTGRVIRV
LVTMFDNSEA KAAQAALSAA IAEVKEANAS KSRFLAAMSH EIRTPMNAIL GFAQLLKMSD
LDDKRRAHVD AIQSAGGTLM NLLTDLLDLS QMEAGHIKIE AKPFDLDDFL GQLADWWQTA
AADKGLRLRI AKDQGLPGCI ISDKGRIQQV LNNFLGNAVK FTEQGRITLA IEEIAHHGAH
RRIRFEVSDT GPGLSDAQTE RLFQPFVQVG ADCSNERGGW GLGLSICHQI ATAMGGTVGV
ASRVGVGSTF HFEVDVGTPA PLSDDPGGSD GTGCERDEPR RGGATDDPAG LHILVAEDNP
ASRTMMREML TELGHRVTTT PDGLAAVREI ESQPFDMVFM DVAMPQLDGL GATRLIRSAP
PPRHVTPIIG CSAHIADPGR FRAAGMDDFL PKPVDRDRLQ HLIRQFAPQT RGGDGGGSDA
R
//
