RADA_MYCTU
ID RADA_MYCTU Reviewed; 480 AA.
AC P9WHJ9; L0TCZ7; O53570; P65953;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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};
DE AltName: Full=DNA repair protein Sms;
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; OrderedLocusNames=Rv3585;
GN ORFNames=MTV024.03;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP INTERACTION WITH DISA.
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.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
CC -!- SUBUNIT: Interacts with DisA (PubMed:23760274).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR EMBL; AL123456; CCP46408.1; -; Genomic_DNA.
DR PIR; B70804; B70804.
DR RefSeq; NP_218102.1; NC_000962.3.
DR RefSeq; WP_003419487.1; NZ_NVQJ01000014.1.
DR AlphaFoldDB; P9WHJ9; -.
DR SMR; P9WHJ9; -.
DR STRING; 83332.Rv3585; -.
DR PaxDb; P9WHJ9; -.
DR DNASU; 887287; -.
DR GeneID; 45427573; -.
DR GeneID; 887287; -.
DR KEGG; mtu:Rv3585; -.
DR TubercuList; Rv3585; -.
DR eggNOG; COG1066; Bacteria.
DR OMA; FELMRLA; -.
DR PhylomeDB; P9WHJ9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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; IBA:GO_Central.
DR CDD; cd01121; Sms; 1.
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..480
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187932"
FT ZN_FING 10..27
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 353..480
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 459..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..258
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 480 AA; 49913 MW; DDECEA049F7099BC CRC64;
MANARSQYRC SECRHVSAKW VGRCLECGRW GTVDEVAVLS AVGGTRRRSV APASGAVPIS
AVDAHRTRPC PTGIDELDRV LGGGIVPGSV TLLAGDPGVG KSTLLLEVAH RWAQSGRRAL
YVSGEESAGQ IRLRADRIGC GTEVEEIYLA AQSDVHTVLD QIETVQPALV IVDSVQTMST
SEADGVTGGV TQVRAVTAAL TAAAKANEVA LILVGHVTKD GAIAGPRSLE HLVDVVLHFE
GDRNGALRMV RGVKNRFGAA DEVGCFLLHD NGIDGIVDPS NLFLDQRPTP VAGTAITVTL
DGKRPLVGEV QALLATPCGG SPRRAVSGIH QARAAMIAAV LEKHARLAIA VNDIYLSTVG
GMRLTEPSAD LAVAIALASA YANLPLPTTA VMIGEVGLAG DIRRVNGMAR RLSEAARQGF
TIALVPPSDD PVPPGMHALR ASTIVAALQY MVDIADHRGT TLATPPSHSG TGHVPLGRGT
