RECA_DEIRA
ID RECA_DEIRA Reviewed; 363 AA.
AC P42443; O32510;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=DR_2340;
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=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=8163172; DOI=10.1016/0378-1119(94)90124-4;
RA Gutman P.D., Carroll J.D., Masters C.I., Minton K.W.;
RT "Sequencing, targeted mutagenesis and expression of a recA gene required
RT for the extreme radioresistance of Deinococcus radiodurans.";
RL Gene 141:31-37(1994).
RN [2]
RP SEQUENCE REVISION.
RA Carroll J.D.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT REC30.
RC STRAIN=KD8301;
RX PubMed=10606814; DOI=10.1016/s0921-8777(99)00048-8;
RA Narumi I., Satoh K., Kikuchi M., Funayama T., Kitayama S., Yanagisawa T.,
RA Watanabe H., Yamamoto K.;
RT "Molecular analysis of the Deinococcus radiodurans recA locus and
RT identification of a mutation site in a DNA repair-deficient mutant,
RT rec30.";
RL Mutat. Res. 435:233-243(1999).
RN [4]
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 [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=20451472; DOI=10.1016/j.dnarep.2010.04.006;
RA Xu G., Lu H., Wang L., Chen H., Xu Z., Hu Y., Tian B., Hua Y.;
RT "DdrB stimulates single-stranded DNA annealing and facilitates RecA-
RT independent DNA repair in Deinococcus radiodurans.";
RL DNA Repair 9:805-812(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=19303848; DOI=10.1016/j.cell.2009.01.018;
RA Slade D., Lindner A.B., Paul G., Radman M.;
RT "Recombination and replication in DNA repair of heavily irradiated
RT Deinococcus radiodurans.";
RL Cell 136:1044-1055(2009).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage (By similarity). Probably involved in base
CC excision repair (PubMed:19303848). {ECO:0000255|HAMAP-Rule:MF_00268,
CC ECO:0000305|PubMed:19303848}.
CC -!- FUNCTION: Following severe irradiation (7 kGy of gamma irradiation)
CC genomic DNA is fragmented. DNA is progressively degraded for the first
CC 1.5 hours after IR, in a step promoted by RecA and counterbalanced by
CC DNA Pol I and Pol III, followed by massive DNA synthesis and genome
CC reassembly in the next hour. Optimal priming of DNA synthesis requires
CC both RecA and RadA, Pol III initiates DNA synthesis while both Pol I
CC and Pol III are required for its contination. In the absence of RecA
CC the majority of the chromosome is still reconstituted, via either
CC single-strand annealing or non-homologous end joining
CC (PubMed:19303848). {ECO:0000269|PubMed:19303848}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- DISRUPTION PHENOTYPE: Reduced DNA synthesis rate even in the absence of
CC ionizing radiation (IR) (PubMed:19303848). Cells lacking this gene have
CC a reduced capacity to survive IR (from 90% survival to <10(-7)), DNA
CC repair following IR is slow (PubMed:20451472, PubMed:19303848). Single
CC recA mutants rarely reconstitutes the whole genome following IR, and
CC their DNA is not degraded post-IR (PubMed:19303848). A double recA-ddrB
CC disruption shows no signs of DNA repair 24 hours after IR
CC (PubMed:20451472). Double recA-radA deletion mutants have a more severe
CC effect than either mutation alone after IR (PubMed:19303848).
CC {ECO:0000269|PubMed:19303848, ECO:0000269|PubMed:20451472}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; U01876; AAC33148.1; -; Genomic_DNA.
DR EMBL; AB005471; BAA21330.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF11887.1; -; Genomic_DNA.
DR PIR; C75285; C75285.
DR RefSeq; NP_296061.1; NC_001263.1.
DR RefSeq; WP_010888966.1; NZ_CP015081.1.
DR PDB; 1XP8; X-ray; 2.50 A; A=1-363.
DR PDBsum; 1XP8; -.
DR AlphaFoldDB; P42443; -.
DR SMR; P42443; -.
DR STRING; 243230.DR_2340; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR EnsemblBacteria; AAF11887; AAF11887; DR_2340.
DR KEGG; dra:DR_2340; -.
DR PATRIC; fig|243230.17.peg.2571; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_0; -.
DR InParanoid; P42443; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR EvolutionaryTrace; P42443; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IMP:CACAO.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..363
FT /note="Protein RecA"
FT /id="PRO_0000122700"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT VARIANT 224
FT /note="G -> S (in rec30; DNA-repair deficient)"
FT HELIX 17..33
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1XP8"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1XP8"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:1XP8"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 252..265
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:1XP8"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1XP8"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:1XP8"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:1XP8"
SQ SEQUENCE 363 AA; 38145 MW; DEF379CF0EF59D74 CRC64;
MSKDATKEIS APTDAKERSK AIETAMSQIE KAFGKGSIMK LGAESKLDVQ VVSTGSLSLD
LALGVGGIPR GRITEIYGPE SGGKTTLALA IVAQAQKAGG TCAFIDAEHA LDPVYARALG
VNTDELLVSQ PDNGEQALEI MELLVRSGAI DVVVVDSVAA LTPRAEIEGD MGDSLPGLQA
RLMSQALRKL TAILSKTGTA AIFINQVREK IGVMYGNPET TTGGRALKFY ASVRLDVRKI
GQPTKVGNDA VANTVKIKTV KNKVAAPFKE VELALVYGKG FDQLSDLVGL AADMDIIKKA
GSFYSYGDER IGQGKEKTIA YIAERPEMEQ EIRDRVMAAI RAGNAGEAPA LAPAPAAPEA
AEA
