ID A0A0Q8QL50_9SPHN Unreviewed; 828 AA.
AC A0A0Q8QL50;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE00_07280 {ECO:0000313|EMBL:KRB86493.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB86493.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB86493.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB86493.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB86493.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB86493.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB86493.1}.
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DR EMBL; LMIB01000001; KRB86493.1; -; Genomic_DNA.
DR RefSeq; WP_056378584.1; NZ_LMIB01000001.1.
DR AlphaFoldDB; A0A0Q8QL50; -.
DR STRING; 1736594.ASE00_07280; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000051854; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR007891; CHASE3.
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; IPR035965; PAS-like_dom_sf.
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; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRB86493.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW Transferase {ECO:0000313|EMBL:KRB86493.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..283
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 359..578
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 589..702
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 711..820
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 638
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 759
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 828 AA; 89772 MW; 00448664C687EE4D CRC64;
MILARPPSPR IRPSWRFVAL LALIGPALLA VMALFLGGEI RSARNAGVAA GKSVEYNLAV
AELLSLLKDA ETGQRGYLIS SDKAFLAPYI EARSHFREQW ANVIRLTPAD GPDADDLRRA
DRLIHAKFTE MQALIDLHDR TGPAAAATRL RAGVGKGLMD EIRAIFARIE KRGRTNLHAI
QNHQNARSER TRMVIWAYVA ITALSAAIAG LLIGRGMRIR NRLGQEYQEA ATRQTAIFEG
TTDAIIVINP SGSIETINPA AEQMFGFQPD DLLRRDISTL IDIAPGEGPF LERIGIDKGR
LRKTEMLDVS GRDSQGETLS VDITLGTMRL PDGLHIIAAL RDAASRKEVD RLKDDFISTV
SHELRTPLTS VVGSLGLLRS GAAGELPAQA QRLAEIAETN SQRLIRLIND ILDIDQIRKG
RMAFDYAVVD LRDVMTRTVQ AMQGLADRRS IKIAMAMPDE PVMACADAER LIQVASNLLS
NAIKFSPEGS AITFDLIGGG DDHIIQITDR GPGIDPDFAR HIFNRFAQGA RPDRKMIAGT
GLGLAISREI VRNHGGDISF ENRAEGGARF AFSVPRDSAQ VVEGDRSARL LICEDDSDAG
FTIQSILTAH GYASDLVTTV RDGIAHARSQ TYKAVLLDLT LADSDGTDLM RALKADKGTQ
QLPVIVISGT PPTGEIDSNS YAGWLQKPFD PPRLIQLIQR ALRRAGARKA VILHVDDDDD
TRELFSTALA GRGLLLSAAS LAAARTILAA RRPDVVVLDL GLPDGSGEDL LVELKRSDQP
LPVILYSAQE VDKKAGALAD AVIIKSRRAL PKLASTVLDI VDRHGGPQ
//
