ID A0A417YL55_9BACI Unreviewed; 459 AA.
AC A0A417YL55;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 17.
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 ECO:0000313|EMBL:RHW33873.1};
GN ORFNames=D1B31_20040 {ECO:0000313|EMBL:RHW33873.1};
OS Neobacillus notoginsengisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1578198 {ECO:0000313|EMBL:RHW33873.1, ECO:0000313|Proteomes:UP000284416};
RN [1] {ECO:0000313|EMBL:RHW33873.1, ECO:0000313|Proteomes:UP000284416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30743 {ECO:0000313|EMBL:RHW33873.1,
RC ECO:0000313|Proteomes:UP000284416};
RX PubMed=28786779; DOI=10.1099/ijsem.0.001975;
RA Zhang M.Y., Cheng J., Cai Y., Zhang T.Y., Wu Y.Y., Manikprabhu D., Li W.J.,
RA Zhang Y.X.;
RT "Bacillus notoginsengisoli sp. nov., a novel bacterium isolated from the
RT rhizosphere of Panax notoginseng.";
RL Int. J. Syst. Evol. Microbiol. 67:2581-2585(2017).
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:0000256|RuleBase:RU003555}.
CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC involving stabilizing or processing branched DNA or blocked replication
CC 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 to
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHW33873.1}.
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DR EMBL; QWEG01000016; RHW33873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417YL55; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000284416; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR CDD; cd01121; RadA_SMS_N; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR NCBIfam; TIGR00416; sms; 1.
DR PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR PANTHER; PTHR32472:SF10; DNA REPAIR PROTEIN RADA-LIKE PROTEIN; 1.
DR Pfam; PF13481; AAA_25; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR PRINTS; PR01874; DNAREPAIRADA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 70..219
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 355..459
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 256..260
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 459 AA; 49859 MW; BF96F6BD8E659694 CRC64;
MAKRKTKFMC TECGYESPKW MGKCPGCGEW NKMVEEVEPA STGRRGAFAH SQGTAVASKA
MPITEVETVT EPRIYTNMTE LNRVLGGGVV KGSLVLIGGD PGIGKSTLLL QVSSQLANKG
HKVLYISGEE SLRQTKLRAE RLGVASGNLF VYAETNLEEI SRTIEQTNPE FVIVDSIQTV
FHPEVTSAPG SVSQVRECTA ELMRIGKTKG IAIFIVGHVT KEGNIAGPRL LEHMVDTVLY
FEGERHHTYR ILRAVKNRFG STNEMGIFEM KEEGLEEVEN PSEIFLEERS RGAAGSTVVA
SMEGTRPVLV EIQALISPTS FGNPRRMATG IDHNRVPLLM AVLEKRVGML LQNQDAYLKV
AGGVKLDEPA IDLAVAVSIA SSFRDQPTRP TDCIIGEVGL TGEVRRVSRI EQRVQEAAKL
GFERVILPAN NLGGWTGPKG LELIGVSTVS DALRAALGE
//
