ID A0A0A1DL23_NOCSI Unreviewed; 457 AA.
AC A0A0A1DL23;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 2.
DT 27-MAR-2024, entry version 39.
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:GEB12297.1};
GN ORFNames=KR76_03515 {ECO:0000313|EMBL:AIY16060.2}, NSI01_06120
GN {ECO:0000313|EMBL:GEB12297.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY16060.2, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY16060.2, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY16060.2,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:GEB12297.1, ECO:0000313|Proteomes:UP000318936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB12297.1,
RC ECO:0000313|Proteomes:UP000318936};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP009896; AIY16060.2; -; Genomic_DNA.
DR EMBL; BJMC01000005; GEB12297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1DL23; -.
DR STRING; 2045.KR76_03515; -.
DR KEGG; psim:KR76_03515; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_11; -.
DR Proteomes; UP000030300; Chromosome.
DR Proteomes; UP000318936; 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 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 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|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:UP000030300};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 46..195
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 331..457
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 232..236
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 457 AA; 47855 MW; 5D9BFE93E6DF1A93 CRC64;
MGRCGECQAW GSVSEVAVAA AGVSSRTAAA PVTTAAVPIA QVSADRAVHH PSGVAELDRV
LGGGLVPGAA VLLAGEPGVG KSTLLLEVAA RTAAGSRRTL YVTGEESAAQ VRLRADRTNA
LEDQLYLAAE TDLGAVLTHI EEVRPATVVI DSVQTISASG VEGVPGGVTQ VKEVAQALVR
MAKSRDITIV MIGHVTKDGG IAGPRVLEHL VDVVLHFEGD RNSRFRMLRA VKNRFGPVDE
VGCFDLGPDG IRAVDDPTGI FVERHHGRVP GTCIAVSMEG RRPLLAEVQG LVTISPNERP
RRTTSGIDSS RLAMVLAVLQ QHCDVRLHQH DVFASTVGGA RLTDPAADLA LAVAVASAHF
VSAPPAGVVA MGEIGLSGEL RRVRDLPQRL AEAARLGFAL AIVPADPGTA QGVRRPSSDR
MIDGMRVIEA PDVISALRLL NLDRRTKHAL EVIDGSE
//
