ID A0A257J3U4_9PROT Unreviewed; 708 AA.
AC A0A257J3U4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=CFE28_06545 {ECO:0000313|EMBL:OYU69688.1};
OS Alphaproteobacteria bacterium PA2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=2015570 {ECO:0000313|EMBL:OYU69688.1, ECO:0000313|Proteomes:UP000215921};
RN [1] {ECO:0000313|EMBL:OYU69688.1, ECO:0000313|Proteomes:UP000215921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA2 {ECO:0000313|EMBL:OYU69688.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
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}.
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:OYU69688.1}.
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DR EMBL; NKIZ01000001; OYU69688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257J3U4; -.
DR Proteomes; UP000215921; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
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; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000215921};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 274..328
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 339..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 579..693
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 628
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 708 AA; 76368 MW; 9BD0DCD2BABAC485 CRC64;
MRPSATPVVV KYRKCLTRVV LPSPRLRMFG RTRAMSMELA RLDALRALEI LDTPPEETFD
QLADLAAEIF DTPMALVSLV DETRQWFKAH PGLKVSETPR EWSFCNHAIQ LGRNGLMVVE
DATLDPRFAA NPLVTGELGL RFYAGAVLTD GNGQNLGTLC VLDTKARSRP PERKLTRLRS
LASLIVRGFE VRQLARRLSE KQSLLGLAER MAGLGHWRVT PGLRTVEWSD EVYNIYGVTR
ETFNPVYGEG IEFHSSEDRL ELGRKFRTAL TTGEPFEYVV RVPAADGSVK VIQGKAEVQR
DDNGRIVSLV GVLQDVTGYE AALNEAADAV SAKSAFLANM SHEIRTPLTS IIGYSELAAS
RPSVGDDIRQ DIGRVHMASQ ALLATVNDIL DFSKLEAGQV TLNLAPVNLA GLAQQTLDIL
ELQADAKGLK LGLTVREGGD GLFSLDRSRV SQILLNLIGN AVKFTASGSV QVNLSRNLEA
GTIRLEVRDT GAGISEEGQA RIFRRFSQID GDTSVGGGTG LGLAICRGLA ATMGGTIGVE
SRLGEGSCFW LEIPAMPALV GAGARIEQAD DDAGLAGVRI LLADDHPVNR ELARLTLVRL
GADVVAVEDG ALALEAEARQ AFDAILLDIR MPVMGGIEAC ERLRARGVVA PIFAFTAEAD
HFDLVSAPGR TFDGVIEKPI NPASMVSTIR AALADEGEDR SEGKVVFL
//
