RQKA_DEIRA
ID RQKA_DEIRA Reviewed; 668 AA.
AC Q9RRH3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DNA damage-responsive serine/threonine-protein kinase RqkA;
DE EC=2.7.11.1;
DE AltName: Full=Radiation and pyrroloquinoline quinone inducible protein kinase;
GN Name=rqkA; OrderedLocusNames=DR_2518;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, INDUCTION,
RP DOMAIN, AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=20633226; DOI=10.1111/j.1365-2958.2010.07301.x;
RA Rajpurohit Y.S., Misra H.S.;
RT "Characterization of a DNA damage-inducible membrane protein kinase from
RT Deinococcus radiodurans and its role in bacterial radioresistance and DNA
RT strand break repair.";
RL Mol. Microbiol. 77:1470-1482(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND MUTAGENESIS OF LYS-42;
RP SER-162; THR-169 AND SER-171.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=23994692; DOI=10.1016/j.biocel.2013.08.011;
RA Rajpurohit Y.S., Misra H.S.;
RT "Structure-function study of deinococcal serine/threonine protein kinase
RT implicates its kinase activity and DNA repair protein phosphorylation roles
RT in radioresistance of Deinococcus radiodurans.";
RL Int. J. Biochem. Cell Biol. 45:2541-2552(2013).
RN [4]
RP FUNCTION IN REGULATION OF GENES, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=22961447; DOI=10.1002/jobm.201100650;
RA Rajpurohit Y.S., Desai S.S., Misra H.S.;
RT "Pyrroloquinoline quinone and a quinoprotein kinase support gamma-radiation
RT resistance in Deinococcus radiodurans and regulate gene expression.";
RL J. Basic Microbiol. 53:518-531(2013).
CC -!- FUNCTION: Plays an important role in radiation resistance and DNA
CC double-strand break (DSB) repair. Involved in transcriptional
CC regulation of genes important for bacterial stress response.
CC Phosphorylates PprA in vitro. {ECO:0000269|PubMed:20633226,
CC ECO:0000269|PubMed:22961447, ECO:0000269|PubMed:23994692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:20633226, ECO:0000269|PubMed:23994692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20633226,
CC ECO:0000269|PubMed:23994692};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:20633226};
CC -!- ACTIVITY REGULATION: Autokinase activity is stimulated by DNA damage.
CC Stimulated by PQQ and DNA ends in vitro. {ECO:0000269|PubMed:20633226}.
CC -!- INDUCTION: Expression is induced in response to DNA damage.
CC {ECO:0000269|PubMed:20633226}.
CC -!- DOMAIN: Contains an N-terminal catalytic kinase domain and a C-terminal
CC PQQ binding domain. {ECO:0000269|PubMed:20633226}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits higher sensitivity to different
CC DNA-damaging agents. It shows altered phosphoprotein profile and
CC impaired DSB repair. Deletion affects expression of genes involved in
CC intermediary metabolism, stress response and growth under stressed
CC conditions. {ECO:0000269|PubMed:20633226, ECO:0000269|PubMed:22961447}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AE000513; AAF12057.1; -; Genomic_DNA.
DR PIR; C75264; C75264.
DR RefSeq; NP_296238.1; NC_001263.1.
DR RefSeq; WP_010889143.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RRH3; -.
DR SMR; Q9RRH3; -.
DR STRING; 243230.DR_2518; -.
DR EnsemblBacteria; AAF12057; AAF12057; DR_2518.
DR KEGG; dra:DR_2518; -.
DR PATRIC; fig|243230.17.peg.2760; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_020359_0_0_0; -.
DR InParanoid; Q9RRH3; -.
DR OMA; PKWRFQA; -.
DR OrthoDB; 1377603at2; -.
DR BRENDA; 2.7.11.1; 1856.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025666; PQQ-like_dom.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 1.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF50998; SSF50998; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..668
FT /note="DNA damage-responsive serine/threonine-protein
FT kinase RqkA"
FT /id="PRO_0000429795"
FT DOMAIN 13..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 42
FT /note="K->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:23994692"
FT MUTAGEN 162
FT /note="S->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:23994692"
FT MUTAGEN 169
FT /note="T->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:23994692"
FT MUTAGEN 171
FT /note="S->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:23994692"
SQ 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
