ID A0A2N4YMK0_9RHOB Unreviewed; 1236 AA.
AC A0A2N4YMK0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C0V75_04770 {ECO:0000313|EMBL:PLL14731.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL14731.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL14731.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL14731.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-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:PLL14731.1}.
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DR EMBL; PKRQ01000001; PLL14731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4YMK0; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000234539; 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; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 5.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 3.
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; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF12860; PAS_7; 1.
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; 3.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000234539}.
FT DOMAIN 311..388
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 383..437
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 666..719
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 720..765
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 869..1086
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1110..1234
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 421..455
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1164
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1236 AA; 135891 MW; A6D79775785ED396 CRC64;
MFMNLRGWRS RDFPAGAVQE VGVPEEISVV RMLNELVRTP LPNLDQAVTR SIGRLAEVSG
AGWACLFRME DGHLRKRFSY MAPGLSPVTC DQDLLVQPFL PDLTANLPAY VADRTALPDD
HPLKEVLACG ALLALPINED GRLTGVLAFV YATPRTDFGP LQIDRMKAAA EVLETVLARR
ETERRYLDTT RRLEATLAAL PDLLFEVTAD GRFAEFVAGP AHLMIAPPEA LRGKSFAELL
PQKVAKLVQG ALEQALATGR VDGVRYRLDL PDGPHWFELT GAVKPSDTPD TQPSVIFLVR
DVTADTRMRD ELTQLGKIVE SMSNLVCIID LDENIVWCNA AFERQTGWTL EEVRGRYLGD
IVRAPGIDPM NAEAVHDAIR LREAYSGTTI NQDRWGNRYW IDFNVVPLHD AQGDLAGFVT
IETVVTQLKE QEAAMAELAR SATEARERLE NAVRALPDAV IIVDDKERVV VANSAYHEMV
PQLAPFAGEG ASLESILRKG VELGVFGPCE TEEEREAWVA KRMAAYRKPF DQDEIQLPDG
RWMRRLHTRT SDGGIVAIAI DVTARHNQIA ALDAANQELS AALAERDQAE RNLRSIIDGA
AVGTWEWDIS ADVLHVGGRW AEMLGRTAAE PGVFSLAEFR ASVHPEDVTL LPNPFRTEMG
TDDSFSEIEF RLRHDDGGWT WVLSRSQVTE RAADGTPLRM AGVHLDISDR KRLERQLQTG
RAYLSEVMDT SIAALAVLNE RGAITYANQE AERILRLERS QLRGRAYNDP GWKLQRVDGS
PLPDDELPFR LAMAQGGIVR DIRFAVHLAD GTRRVLSANA VPLTPLDGGQ QVVVSFSDIT
DELASTARLE EARSRAEEMS RAKSIFLANM SHEIRTPLNG VLGMAEVLDS IVEVPEQKQM
VATIRRSGET LLTVLNSILD MSKIEAGKMV LEEVPMVLSD VLAQVEALHR VKAEEKGLEL
QVLTSAGADL PRMGDPHRLT QILNNLLSNA IKFTEQGRVR LKLSCKPGKP INIDVSDTGV
GMTEIQLSRV FESFEQADGS MTRRFGGTGL GLSIVRQLVL LMGGMISLQS RPGEGTQVRV
VIPLAEAAIG SVAGPEPDEA PDLTALNGRN LLIADDNVTN RMVLAEMLGQ TGLRTTMVEN
GQEAVVAWER AQAQASPFDL LLLDITMPVM DGLRALAEIR DREGRGGVDP VPAIAVTANA
MPNQVADYIM GGFDTHLAKP FKRKELLHAV KTLLRN
//
