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DNA damage-responsive serine/threonine-protein kinase RqkA (EC 2.7.11.1) (Radiation and pyrroloquinoline quinone inducible protein kinase)

 RQKA_DEIRA              Reviewed;         668 AA.
Q9RRH3;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 135.
RecName: Full=DNA damage-responsive serine/threonine-protein kinase RqkA;
EC=2.7.11.1;
AltName: Full=Radiation and pyrroloquinoline quinone inducible protein kinase;
Name=rqkA; OrderedLocusNames=DR_2518;
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 /
LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
Deinococcaceae; Deinococcus.
NCBI_TaxID=243230;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
NCIMB 9279 / R1 / VKM B-1422;
PubMed=10567266; DOI=10.1126/science.286.5444.1571;
White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
Fraser C.M.;
"Genome sequence of the radioresistant bacterium Deinococcus
radiodurans R1.";
Science 286:1571-1577(1999).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, INDUCTION,
DOMAIN, AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
NCIMB 9279 / R1 / VKM B-1422;
PubMed=20633226; DOI=10.1111/j.1365-2958.2010.07301.x;
Rajpurohit Y.S., Misra H.S.;
"Characterization of a DNA damage-inducible membrane protein kinase
from Deinococcus radiodurans and its role in bacterial radioresistance
and DNA strand break repair.";
Mol. Microbiol. 77:1470-1482(2010).
[3]
FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND MUTAGENESIS OF LYS-42;
SER-162; THR-169 AND SER-171.
STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
NCIMB 9279 / R1 / VKM B-1422;
PubMed=23994692; DOI=10.1016/j.biocel.2013.08.011;
Rajpurohit Y.S., Misra H.S.;
"Structure-function study of deinococcal serine/threonine protein
kinase implicates its kinase activity and DNA repair protein
phosphorylation roles in radioresistance of Deinococcus radiodurans.";
Int. J. Biochem. Cell Biol. 45:2541-2552(2013).
[4]
FUNCTION IN REGULATION OF GENES, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
NCIMB 9279 / R1 / VKM B-1422;
PubMed=22961447; DOI=10.1002/jobm.201100650;
Rajpurohit Y.S., Desai S.S., Misra H.S.;
"Pyrroloquinoline quinone and a quinoprotein kinase support gamma-
radiation resistance in Deinococcus radiodurans and regulate gene
expression.";
J. Basic Microbiol. 53:518-531(2013).
-!- FUNCTION: Plays an important role in radiation resistance and DNA
double-strand break (DSB) repair. Involved in transcriptional
regulation of genes important for bacterial stress response.
Phosphorylates PprA in vitro. {ECO:0000269|PubMed:20633226,
ECO:0000269|PubMed:22961447, ECO:0000269|PubMed:23994692}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20633226, ECO:0000269|PubMed:23994692}.
-!- COFACTOR:
Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
Evidence={ECO:0000269|PubMed:20633226};
-!- ENZYME REGULATION: Autokinase activity is stimulated by DNA
damage. Stimulated by PQQ and DNA ends in vitro.
{ECO:0000269|PubMed:20633226}.
-!- INDUCTION: Expression is induced in response to DNA damage.
{ECO:0000269|PubMed:20633226}.
-!- DOMAIN: Contains an N-terminal catalytic kinase domain and a C-
terminal PQQ binding domain. {ECO:0000269|PubMed:20633226}.
-!- PTM: Autophosphorylated.
-!- DISRUPTION PHENOTYPE: Mutant exhibits higher sensitivity to
different DNA-damaging agents. It shows altered phosphoprotein
profile and impaired DSB repair. Deletion affects expression of
genes involved in intermediary metabolism, stress response and
growth under stressed conditions. {ECO:0000269|PubMed:20633226,
ECO:0000269|PubMed:22961447}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AE000513; AAF12057.1; -; Genomic_DNA.
PIR; C75264; C75264.
RefSeq; NP_296238.1; NC_001263.1.
RefSeq; WP_010889143.1; NZ_CP015081.1.
ProteinModelPortal; Q9RRH3; -.
STRING; 243230.DR_2518; -.
EnsemblBacteria; AAF12057; AAF12057; DR_2518.
GeneID; 1798368; -.
KEGG; dra:DR_2518; -.
PATRIC; fig|243230.17.peg.2760; -.
eggNOG; ENOG4107QPV; Bacteria.
eggNOG; COG0515; LUCA.
eggNOG; COG1520; LUCA.
HOGENOM; HOG000099391; -.
InParanoid; Q9RRH3; -.
KO; K12132; -.
OMA; RFRMSND; -.
OrthoDB; POG091H0264; -.
Proteomes; UP000002524; Chromosome I.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR018391; PQQ_beta_propeller_repeat.
InterPro; IPR002372; PQQ_repeat.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF00069; Pkinase; 1.
Pfam; PF13360; PQQ_2; 2.
SMART; SM00564; PQQ; 7.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase.
CHAIN 1 668 DNA damage-responsive serine/threonine-
protein kinase RqkA.
/FTId=PRO_0000429795.
DOMAIN 13 272 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 19 27 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 137 137 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 42 42 ATP. {ECO:0000305}.
MUTAGEN 42 42 K->A: Lack of activity.
{ECO:0000269|PubMed:23994692}.
MUTAGEN 162 162 S->A: Almost no change in activity.
{ECO:0000269|PubMed:23994692}.
MUTAGEN 169 169 T->A: Strong decrease in activity.
{ECO:0000269|PubMed:23994692}.
MUTAGEN 171 171 S->A: Strong decrease in activity.
{ECO:0000269|PubMed:23994692}.
SEQUENCE 668 AA; 71126 MW; 22997D8E4127BC92 CRC64;
MPLTPGTLLA GRYELLALLG EGGSAQVYRA QDGLLGREVA LKVMHDYLPE SDRSRFLREV
RTLARLTHPG VVPVLDLGQE PEAGRPFFTM PLLTGGPITR LGPLEDAPGP LARFLTAAAF
ASRALHHVHS HGIVHRDLTP GNVLLDDTGL PRIMDFGLVA LSEQTRHLTR SGVTLGTPAY
MAPEQAKGGG VDARSDLYAL GAVLYRVACG SPPFVGDSDQ SVLYQHVYEP VPDPRDLNPA
VPDAVARVLL WLLAKRADRR PQSGAALAHL WALARRDLWT THARGQYRGG RARTGEHPDG
PARVSDMQEL WSVALPGEVT WPAAVVGEGD LVAVGTRGGQ LVLTHTSGRP FATYAARDEV
TAPATLIGGH VLYGAWDGTL RRVELQSGSE VWRHQARAEF TGAPTVWGGR LLAPSRDGHL
HALSLRTGEL AWAYRAGGSL AASPLVWAGA ALQCDETGWL HALDARSGTP LWKVEVGTVH
ATPALLPGPP GTATLVIATW EGEVHAIGLE VQNGRAALAG EDAIRWTYDV EDEVWASPAL
TALDLPPDSG AAPDASAAPG GVVVVAGWGG KVRGLRLADG EDLWERTLDG RVTASPVISA
GLVFLATEGG ELLALDVRNG EVRWTCRERS GVQATPLAAS GTLYVAFMDG TLRAYRNAHP
EWRSEQEG


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