ID Q162F3_ROSDO Unreviewed; 722 AA.
AC Q162F3;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Polar-differentiation response regulator DivK {ECO:0000256|ARBA:ARBA00039809};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=torS {ECO:0000313|EMBL:ABG33140.1};
GN OrderedLocusNames=RD1_3666 {ECO:0000313|EMBL:ABG33140.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG33140.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG33140.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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}.
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DR EMBL; CP000362; ABG33140.1; -; Genomic_DNA.
DR AlphaFoldDB; Q162F3; -.
DR STRING; 375451.RD1_3666; -.
DR KEGG; rde:RD1_3666; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG4192; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_40_2_5; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABG33140.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 123..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..200
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 243..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 486..600
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 535
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 722 AA; 75964 MW; 9EDEA75DEEDB88CE CRC64;
MVDALRLQFQ QVPEITTLAQ MAQIQTELEA GITLAQRRVA YLPSPQAAQE AVALLQRQQQ
AVASGGLTEA SRDRIALRAL IAQDSVLLQN TIAALSERAR QARDLVQAEG LAQIAAAKTR
SSWMLFGLLV VITGAVIAGG LLWVYARRQL VTRLGNISRR IVAVAGGEYG QPVAISGHDE
IGRMEKALNI LRRRAQDAAR LRGHLEEAVI ARTGDVVAEM QASDAARAEA EAANRSKTEF
LARMSHEIRT PLNGIIGMLD LLQADMTDPE AKARTATALN SARDLLDITN DILNFAGGED
SANRGNPVHF PLRELVGQLG HQVQSLAAQK GLEAVVDLSN PAPLVVLGDV VKIRQIVGNL
ISNAVKYTPH GAATLVVDHA MDAQSGQPVL SFTVADTGVG MTREAIAHAF DAYMRTDAAK
RAGIEGLGLG LAISRKLTEA LGGALSIESE VGVGSRFTLT VPVLHGDPAQ VVQEEAPLGD
ACIRRDVLVI DDHAVNLMVA RGYLERLGCR VTVAQTGAAG VQAGRAGRFD LVLIDLDLPD
MGGADVAAAL AQQENAPLLV ALTAHLIEDT PENRQRLGVA RVLSKPVSPR ALAKVLDAGT
TDAVPADYAG VLDSLCGDAA DLGPQITGQI VAEFLDDLPR AVGAILDGPP GSARKSAHRL
KGAAANFRLE SLCAVLARIE AAENGADAAL RSLLKDAAQE AKSVLHRAAQ AAELQIAPGS
TK
//
