ID A0A1M4WYT8_9FIRM Unreviewed; 462 AA.
AC A0A1M4WYT8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
GN ORFNames=SAMN02746064_01364 {ECO:0000313|EMBL:SHE86426.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHE86426.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHE86426.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHE86426.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000256|RuleBase:RU003555}.
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DR EMBL; FQTU01000008; SHE86426.1; -; Genomic_DNA.
DR RefSeq; WP_073270439.1; NZ_FQTU01000008.1.
DR AlphaFoldDB; A0A1M4WYT8; -.
DR STRING; 1120975.SAMN02746064_01364; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000184251; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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|RuleBase:RU003555};
KW DNA damage {ECO:0000256|RuleBase:RU003555};
KW DNA repair {ECO:0000256|RuleBase:RU003555};
KW DNA-binding {ECO:0000256|RuleBase:RU003555};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003555};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003555};
KW Reference proteome {ECO:0000313|Proteomes:UP000184251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 67..220
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
SQ SEQUENCE 462 AA; 51085 MW; E40CB3C6E3B8633A CRC64;
MRTKTVFVCT NCEAESYKWQ GYCSNCGEWN TLEEKTVTKK DDKARKTSGK SSIAKKIQPL
SKVPINSSER IVTGIKEFDR VMGGGVVRDS LSIITAKPGA GKSTLLLQVA GELAQKGLKI
LYASGEESES QIKNRADRIF STIDDNLLVY CDNDLNNVIA NVNEANPDLI ILDSIQTFIM
PDVSDSRAGS PTQTMECANA MLQLAKDTKR PRAVIMVGQM TKKDEMAGLR ALEHLVDAVL
IIEGENEEEL RGLSVSKNRF GSTWERGFFT MSEKGLVSID NPSEFFMTKR DDGELVGGSA
LTVIRDGSRS IIVEVESLVS HSFTPYPSRI CECIPKDQLN TLISVLEQKS GVMLYDKNVV
LKSTGGLRLK EQSVNLCVLM SIVSSVKNKG IPGNTAFVAD VGLTGELKKV PTLEQRIREL
DRMGFDRVFV AKNDVHIKQT YENIKVCQCK NIQDVIRMLF SL
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