(data stored in ACNUC7421 zone)

SWISSPROT: D6XV75_BACIE

ID   D6XV75_BACIE            Unreviewed;       470 AA.
AC   D6XV75;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN   Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN   OrderedLocusNames=Bsel_0084 {ECO:0000313|EMBL:ADH97633.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97633.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97633.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase involved in processing of
CC       recombination intermediates, plays a role in repairing DNA breaks.
CC       Stimulates the branch migration of RecA-mediated strand transfer
CC       reactions, allowing the 3' invading strand to extend heteroduplex
CC       DNA faster. Binds ssDNA in the presence of ADP but not other
CC       nucleotides, has ATPase activity that is stimulated by ssDNA and
CC       various branched DNA structures, but inhibited by SSB. Does not
CC       have RecA's homology-searching function.
CC       {ECO:0000256|RuleBase:RU003555}.
CC   -!- FUNCTION: Plays a role in repairing double-strand DNA breaks,
CC       probably involving stabilizing or processing branched DNA or
CC       blocked replication forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC       including the RadA KNRFG motif, while the C-terminus is homologous
CC       to Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}.
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DR   EMBL; CP001791; ADH97633.1; -; Genomic_DNA.
DR   RefSeq; WP_013171063.1; NC_014219.1.
DR   STRING; 439292.Bsel_0084; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; ADH97633; ADH97633; Bsel_0084.
DR   KEGG; bse:Bsel_0084; -.
DR   eggNOG; ENOG4105DNJ; Bacteria.
DR   eggNOG; COG1066; LUCA.
DR   HOGENOM; HOG000218329; -.
DR   KO; K04485; -.
DR   OMA; SQVREIT; -.
DR   OrthoDB; 505485at2; -.
DR   BioCyc; BSEL439292:G1GLR-108-MONOMER; -.
DR   Proteomes; UP000000271; 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; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; D6XV75.
DR   SWISS-2DPAGE; D6XV75.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01498};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN       71    220       RECA_2. {ECO:0000259|PROSITE:PS50162}.
FT   NP_BIND     100    107       ATP. {ECO:0000256|HAMAP-Rule:MF_01498}.
FT   REGION      356    470       Lon-protease-like. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
FT   MOTIF       257    261       RadA KNRFG motif. {ECO:0000256|HAMAP-
FT                                Rule:MF_01498}.
SQ   SEQUENCE   470 AA;  51283 MW;  F0D009C33522E399 CRC64;
     MAKKKTKFIC QECGYESAKW MGKCPGCSGW NTLVEEMEKP ASSAHEKRSF VTAGGGIRQK
     PQSIMDIEQK EENRVSTYIN ELNRVLGGGI VPGSLVLVGG DPGIGKSTLL LQVSATLSEH
     KKKVLYISGE ESLKQTKLRA NRLGVGNDYL FVHSETDVEY IEQAIDQVNP DLVIIDSIQT
     VYLDHITSAP GSVSQVREST SVFMRIAKTR GIAIFLVGHV TKQGSIAGPR ILEHMVDSVL
     YFEGERHHTY RILRAVKNRF GSTNEIGIFE MKETGLEEVL NPSEIFLEER SSGASGSAVV
     ASMEGTRPVL VEMQSLIAPT SFGNPRRMAT GVDHNRISLI MAVLEKRAGI LLQNHDAYVK
     VAGGVRLDEP SIDLAIAISI VSSFRDQPSR AGDVIIGEVG LTGEIRRVSR IEQRVQEAAK
     LGFERVIIPD RNFGGWTVPD GIEVIGARDI NEAINEALGG RASGAPKFEL
//

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