PPRA_DEIRA
ID PPRA_DEIRA Reviewed; 300 AA.
AC O32504;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=DNA repair protein PprA;
DE AltName: Full=Pleiotropic protein promoting DNA repair;
GN Name=pprA; OrderedLocusNames=DR_A0346;
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 [GENOMIC DNA].
RC STRAIN=KD8301;
RA Narumi I., Du Z., Alatas Z., Kitayama S., Watanabe H.;
RT "Isolation and characterization of pprA, a novel Deinococcus radiodurans
RT gene involved in DNA repair.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP INDUCTION, ROLE IN RADIORESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15454524; DOI=10.1534/genetics.104.029249;
RA Tanaka M., Earl A.M., Howell H.A., Park M.J., Eisen J.A., Peterson S.N.,
RA Battista J.R.;
RT "Analysis of Deinococcus radiodurans's transcriptional response to ionizing
RT radiation and desiccation reveals novel proteins that contribute to extreme
RT radioresistance.";
RL Genetics 168:21-33(2004).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLY-165.
RX PubMed=15458422; DOI=10.1111/j.1365-2958.2004.04272.x;
RA Narumi I., Satoh K., Cui S., Funayama T., Kitayama S., Watanabe H.;
RT "PprA: a novel protein from Deinococcus radiodurans that stimulates DNA
RT ligation.";
RL Mol. Microbiol. 54:278-285(2004).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=16406432; DOI=10.1016/j.mrfmmm.2005.11.006;
RA Satoh K., Wada S., Kikuchi M., Funayama T., Narumi I., Kobayashi Y.;
RT "Method for detecting DNA strand breaks in mammalian cells using the
RT Deinococcus radiodurans PprA protein.";
RL Mutat. Res. 596:36-42(2006).
RN [6]
RP PHOSPHORYLATION AT THR-88; SER-128 AND THR-160, ACTIVITY REGULATION, AND
RP DNA-BINDING.
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).
CC -!- FUNCTION: dsDNA-binding protein that contributes to the ionizing
CC radiation resistance of D.radiodurans. Plays a role in DNA repair and
CC genome reconstitution, and is necessary for recovery from severe
CC genomic fragmentation as a result of exposure to severe levels of
CC ionizing radiation. In vitro, binds to double-stranded DNA carrying
CC strand breaks and stimulates the DNA end-joining reaction catalyzed by
CC DNA ligases. Thus, PprA plays a critical role in a non-homologous end-
CC joining (NHEJ) pathway for the repair of radiation-induced DNA double-
CC strands breaks. Cannot bind to dsDNA without strand breaks or single-
CC stranded DNA. {ECO:0000269|PubMed:15454524,
CC ECO:0000269|PubMed:15458422}.
CC -!- ACTIVITY REGULATION: Phosphorylation increases DNA binding affinity.
CC {ECO:0000269|PubMed:23994692}.
CC -!- INDUCTION: Induced to high levels following extreme ionizing radiation
CC exposure. Also highly induced in response to desiccation stress.
CC {ECO:0000269|PubMed:15454524}.
CC -!- PTM: Phosphorylated by RqkA in vitro. Phosphorylated primarily at Thr-
CC 88, and to a little extent at Ser-128 and Thr-160.
CC {ECO:0000269|PubMed:23994692}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduced growth
CC rate, do not exhibit a decrease in the efficiency of natural
CC transformation, but are much more sensitive to ionizing radiation than
CC the wild-type strain. {ECO:0000269|PubMed:15454524}.
CC -!- BIOTECHNOLOGY: The PprA protein combined with an immunofluorescence
CC technique can be used to visualize radiation-induced DNA strand breaks
CC in mammalian cultured cells, allowing the evaluation of DNA damage
CC responses. This detection method could also be applicable to genotoxic
CC tests in the environmental and pharmaceutical fields.
CC {ECO:0000269|PubMed:16406432}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB003475; BAA21374.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE001825; AAF12437.1; -; Genomic_DNA.
DR PIR; F75589; F75589.
DR RefSeq; NP_285669.1; NC_001264.1.
DR RefSeq; WP_010889605.1; NZ_CP015082.1.
DR PDB; 6A27; X-ray; 1.35 A; A/B=17-300.
DR PDB; 6A28; X-ray; 2.19 A; A/B=17-300.
DR PDB; 6A29; X-ray; 2.40 A; A/B/C/D/E/F/G/H=17-300.
DR PDB; 6BDU; X-ray; 2.00 A; A/B=25-300.
DR PDB; 6MC6; X-ray; 2.75 A; A/B=25-300.
DR PDB; 6NEO; X-ray; 5.94 A; B=25-300.
DR PDBsum; 6A27; -.
DR PDBsum; 6A28; -.
DR PDBsum; 6A29; -.
DR PDBsum; 6BDU; -.
DR PDBsum; 6MC6; -.
DR PDBsum; 6NEO; -.
DR AlphaFoldDB; O32504; -.
DR SMR; O32504; -.
DR STRING; 243230.DR_A0346; -.
DR iPTMnet; O32504; -.
DR EnsemblBacteria; AAF12437; AAF12437; DR_A0346.
DR KEGG; dra:DR_A0346; -.
DR PATRIC; fig|243230.17.peg.3238; -.
DR HOGENOM; CLU_917422_0_0_0; -.
DR OMA; RDFETHW; -.
DR OrthoDB; 1259763at2; -.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0071465; P:cellular response to desiccation; IEP:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0051106; P:positive regulation of DNA ligation; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..300
FT /note="DNA repair protein PprA"
FT /id="PRO_0000058551"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:23994692"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:23994692"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:23994692"
FT MUTAGEN 88
FT /note="T->A: Strong decrease in phosphorylation. Lack of
FT phosphorylation; when associated with A-128 and A-160."
FT MUTAGEN 128
FT /note="S->A: Slight decrease in phosphorylation. Lack of
FT phosphorylation; when associated with A-88 and A-160."
FT MUTAGEN 160
FT /note="T->A: Slight decrease in phosphorylation. Lack of
FT phosphorylation; when associated with A-88 and A-128."
FT MUTAGEN 165
FT /note="G->E: In KH311; loss of radiation resistance and
FT DNA-binding ability."
FT /evidence="ECO:0000269|PubMed:15458422"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6A27"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6A29"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6BDU"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:6A27"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:6BDU"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:6BDU"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:6BDU"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6BDU"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:6A27"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:6A27"
SQ SEQUENCE 300 AA; 32210 MW; 8C635D7A52CC6A60 CRC64;
MLPLAFLICS GHNKGSMARA KAKDQTDGIY AAFDTLMSTA GVDSQIAALA ASEADAGTLD
AALTQSLQEA QGRWGLGLHH LRHEARLTDD GDIEILTDGR PSARVSEGFG ALAQAYAPMQ
ALDERGLSQW AALGEGYRAP GDLPLAQLKV LIEHARDFET DWSAGRGETF QRVWRKGDTL
FVEVARPASA EAALSDAAWD VIASIKDRAF QRELMRRSEK DGMLGALLGA RHAGAKANLA
QLPEAHFTVQ AFVQTLSGAA ARNAEEYRAA LKTAAAALEE YQGVTTRQLS EVLRHGLRES
