(data stored in SCRATCH zone)

SWISSPROT: RADA_BACSU

ID   RADA_BACSU              Reviewed;         458 AA.
AC   P37572;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 137.
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 {ECO:0000303|PubMed:9141693};
GN   Name=radA {ECO:0000255|HAMAP-Rule:MF_01498};
GN   Synonyms=orf5 {ECO:0000303|PubMed:9141693},
GN   sms {ECO:0000303|PubMed:9141693}, yacJ; OrderedLocusNames=BSU00870;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-259.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8016066; DOI=10.1073/pnas.91.13.5788;
RA   Msadek T., Kunst F., Rapoport G.;
RT   "MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a
RT   pleiotropic regulator controlling competence gene expression and growth at
RT   high temperature.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5788-5792(1994).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / IS58;
RX   PubMed=9141693; DOI=10.1099/00221287-143-4-1309;
RA   Krueger E., Msadek T., Ohlmeier S., Hecker M.;
RT   "The Bacillus subtilis clpC operon encodes DNA repair and competence
RT   proteins.";
RL   Microbiology 143:1309-1316(1997).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=11810266; DOI=10.1007/s00438-001-0616-7;
RA   Carrasco B., Fernandez S., Asai K., Ogasawara N., Alonso J.C.;
RT   "Effect of the recU suppressors sms and subA on DNA repair and homologous
RT   recombination in Bacillus subtilis.";
RL   Mol. Genet. Genomics 266:899-906(2002).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=15317759; DOI=10.1128/jb.186.17.5557-5566.2004;
RA   Carrasco B., Cozar M.C., Lurz R., Alonso J.C., Ayora S.;
RT   "Genetic recombination in Bacillus subtilis 168: contribution of Holliday
RT   junction processing functions in chromosome segregation.";
RL   J. Bacteriol. 186:5557-5566(2004).
RN   [7]
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).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168, 168 / PY79, and 168 / YB886 / BG214;
RX   PubMed=25616256; DOI=10.1016/j.dnarep.2014.12.007;
RA   Gandara C., Alonso J.C.;
RT   "DisA and c-di-AMP act at the intersection between DNA-damage response and
RT   stress homeostasis in exponentially growing Bacillus subtilis cells.";
RL   DNA Repair 27:1-8(2015).
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   -!- FUNCTION: Plays a role in DNA repair (PubMed:9141693, PubMed:11810266).
CC       Might stabilize or process Holliday junction intermediates
CC       (PubMed:15317759). May work with DisA following methyl methanesulfonate
CC       (MMS) but not H(2)O(2) damage; DisA is a DNA integrity scanning protein
CC       with c-di-AMP synthase activity. {ECO:0000269|PubMed:15317759,
CC       ECO:0000269|PubMed:9141693}.
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   -!- DISRUPTION PHENOTYPE: General sensitivity to DNA damaging agents.
CC       Increased sensitivity to methyl methanesulfonate (MMS), decreased
CC       survival after UV irradiation in transition and stationary phase,
CC       decrease in transformation with chromosomal DNA requiring homologous
CC       recombination (PubMed:9141693, PubMed:11810266). Increased sensitivity
CC       to mitomycin C, H(2)O(2), and nalidixic acid; a further disA deletion
CC       suppresses H(2)O(2) sensitivity but has no effect on MMS sensitivity,
CC       suggesting radA and disA might work in the same DNA repair pathway
CC       (PubMed:25616256). Partially suppresses DNA damaging agent sensitivity
CC       of recU deletions (PubMed:11810266). Suppresses a chromosome
CC       segregation defect in ruvA and recD mutants cells, but not in recU
CC       mutant cells (PubMed:15317759). {ECO:0000269|PubMed:11810266,
CC       ECO:0000269|PubMed:15317759, ECO:0000269|PubMed:25616256,
CC       ECO:0000269|PubMed:9141693}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01498}.
DR   EMBL; D26185; BAA05321.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11863.1; -; Genomic_DNA.
DR   EMBL; U02604; AAA19234.1; -; Unassigned_DNA.
DR   PIR; S66116; S66116.
DR   RefSeq; NP_387968.1; NC_000964.3.
DR   RefSeq; WP_004399687.1; NZ_JNCM01000029.1.
DR   SMR; P37572; -.
DR   STRING; 224308.BSU00870; -.
DR   MEROPS; S16.A04; -.
DR   PaxDb; P37572; -.
DR   PRIDE; P37572; -.
DR   EnsemblBacteria; CAB11863; CAB11863; BSU00870.
DR   GeneID; 936872; -.
DR   KEGG; bsu:BSU00870; -.
DR   PATRIC; fig|224308.179.peg.88; -.
DR   eggNOG; ENOG4105DNJ; Bacteria.
DR   eggNOG; COG1066; LUCA.
DR   HOGENOM; HOG000218329; -.
DR   InParanoid; P37572; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   PhylomeDB; P37572; -.
DR   BioCyc; BSUB:BSU00870-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro.
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   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;
DR   PRODOM; P37572.
DR   SWISS-2DPAGE; P37572.
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..458
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187921"
FT   ZN_FING         10..27
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   NP_BIND         98..105
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          354..458
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           255..259
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   458 AA;  49483 MW;  7397601CF42C801B CRC64;
     MAKTKSKFIC QSCGYESPKW MGKCPGCGAW NTMVEEMIKK APANRRAAFS HSVQTVQKPS
     PITSIETSEE PRVKTQLGEF NRVLGGGVVK GSLVLIGGDP GIGKSTLLLQ VSAQLSGSSN
     SVLYISGEES VKQTKLRADR LGINNPSLHV LSETDMEYIS SAIQEMNPSF VVVDSIQTVY
     QSDITSAPGS VSQVRECTAE LMKIAKTKGI PIFIVGHVTK EGSIAGPRLL EHMVDTVLYF
     EGERHHTFRI LRAVKNRFGS TNEMGIFEMR EEGLTEVLNP SEIFLEERSA GSAGSSITAS
     MEGTRPILVE IQALISPTSF GNPRRMATGI DHNRVSLLMA VLEKRVGLLL QNQDAYLKVA
     GGVKLDEPAI DLAIVISIAS SFRDTPPNPA DCFIGEVGLT GEVRRVSRIE QRVKEAAKLG
     FKRMIIPAAN LDGWTKPKGI EVIGVANVAE ALRTSLGG
//

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