RADA_MYCS2
ID RADA_MYCS2 Reviewed; 466 AA.
AC A0R563;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498};
DE AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498};
GN OrderedLocusNames=MSMEG_6079, MSMEI_5919;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS AN ANTAGONIST OF DISA, OPERON STRUCTURE, AND INTERACTION WITH
RP DISA.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23760274; DOI=10.1074/jbc.m113.464883;
RA Zhang L., He Z.G.;
RT "Radiation-sensitive gene A (RadA) targets DisA, DNA integrity scanning
RT protein A, to negatively affect cyclic di-AMP synthesis activity in
RT Mycobacterium smegmatis.";
RL J. Biol. Chem. 288:22426-22436(2013).
CC -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination
CC intermediates, plays a role in repairing DNA breaks. Stimulates the
CC branch migration of RecA-mediated strand transfer reactions, allowing
CC the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA
CC in the presence of ADP but not other nucleotides, has ATPase activity
CC that is stimulated by ssDNA and various branched DNA structures, but
CC inhibited by SSB. Does not have RecA's homology-searching function (By
CC similarity). Also inhibits the diadenylate cyclase activity of DisA
CC (PubMed:23760274). {ECO:0000255|HAMAP-Rule:MF_01498,
CC ECO:0000269|PubMed:23760274}.
CC -!- SUBUNIT: Interacts with DisA. {ECO:0000269|PubMed:23760274}.
CC -!- INDUCTION: Forms part of an operon with disA.
CC {ECO:0000269|PubMed:23760274}.
CC -!- DOMAIN: Has a putative N-terminal zinc-finger, a middle region with
CC homology to RecA with ATPase motifs including the RadA KNRFG motif,
CC while the C-terminus is homologous to Lon protease. {ECO:0000255|HAMAP-
CC Rule:MF_01498}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR EMBL; CP000480; ABK69709.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42352.1; -; Genomic_DNA.
DR RefSeq; WP_011731022.1; NZ_SIJM01000046.1.
DR RefSeq; YP_890301.1; NC_008596.1.
DR AlphaFoldDB; A0R563; -.
DR SMR; A0R563; -.
DR STRING; 246196.MSMEI_5919; -.
DR MEROPS; S16.004; -.
DR EnsemblBacteria; ABK69709; ABK69709; MSMEG_6079.
DR EnsemblBacteria; AFP42352; AFP42352; MSMEI_5919.
DR GeneID; 66737363; -.
DR KEGG; msg:MSMEI_5919; -.
DR KEGG; msm:MSMEG_6079; -.
DR PATRIC; fig|246196.19.peg.5917; -.
DR eggNOG; COG1066; Bacteria.
DR OMA; FELMRLA; -.
DR OrthoDB; 505485at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01498; RadA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00416; sms; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..466
FT /note="DNA repair protein RadA"
FT /id="PRO_0000424182"
FT ZN_FING 12..29
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 359..466
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 261..265
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 466 AA; 48332 MW; 231581C9A80EBB15 CRC64;
MAGSKIRSQY RCSECQHVAP KWVGRCANCG TWGTVDEVAV LAGNNKLNGA ARRSVAPTSP
AVPITSIDPG VTRHYPTGVS ELDRVLGGGL VAGSVTLLAG DPGVGKSTLL LEVANRWAHS
GKRALYLSGE ESAGQIRLRA ERTGCTHDQV YLAAESDLQI ALGHIDEVKP SLVVVDSVQT
MSTTEADGVT GGVTQVRAVT TSLTAYAKAA VGDPAVAMIL VGHVTKDGAI AGPRSLEHLV
DVVLHFEGDR ASSLRMVRGV KNRFGAADEV GCFQLHDNGI ECVSDPSGLF LDQRPLAVPG
TAVTVTLDGK RPMIGEVQAL VSPPAGPPRR AVSGIDSARA AMIGAVLQTR CRMPINSNDL
YLSTVGGMRL TDPSADLAVA LAIASAYFDI AMPMKAIAIG EVGLAGDLRR VTGMDRRLSE
AARLGFTTAV VPPGVTSAPA GLKVVAADNI RAAVQTMREI AIAGAQ
