ID U7UUB5_9FIRM Unreviewed; 449 AA.
AC U7UUB5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
GN Name=radA {ECO:0000313|EMBL:ERT62886.1};
GN ORFNames=HMPREF1252_0980 {ECO:0000313|EMBL:ERT62886.1};
OS Peptoniphilus sp. BV3AC2.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1111133 {ECO:0000313|EMBL:ERT62886.1, ECO:0000313|Proteomes:UP000017087};
RN [1] {ECO:0000313|EMBL:ERT62886.1, ECO:0000313|Proteomes:UP000017087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3AC2 {ECO:0000313|EMBL:ERT62886.1,
RC ECO:0000313|Proteomes:UP000017087};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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}.
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:ERT62886.1}.
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DR EMBL; AWXD01000031; ERT62886.1; -; Genomic_DNA.
DR RefSeq; WP_023060193.1; NZ_AWXD01000031.1.
DR AlphaFoldDB; U7UUB5; -.
DR PATRIC; fig|1111133.4.peg.1576; -.
DR Proteomes; UP000017087; 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 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 60..212
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
SQ SEQUENCE 449 AA; 49534 MW; CC6F916000FA2613 CRC64;
MYKCSECGYT SPGFLGKCPE CGAWGSMEET KEEKKTKSVS KTEIFKSKGS KPLKDVEALE
GERILTGVSE FDRVMGGGIL KDSLTILTAR PGAGKSTLLL QVSNILASKG KKVLYASGEE
SASQIRQRAK RIVENISDNL FVISTNNLVD VLDEVESLDC DFVIVDSIQT FIIPNIESRA
GSPTQIMESI HILMNMAKNE TRPRAVFIVG QMTKEDSLAG VRSLEHAVDT VLLLSGETYE
ELRILSTTKN RYGSTGEMGF FKMDEKGLTS IDNPSEYFMT ERENGKNVPG SALSVTREGT
RPIILEVESL VSKSFMPYPS RVSEHLRKEQ LFTLISILEE RGEVPMMDKN VVVKTTGGIK
LQDTASNLSV IVSIYSSLVG KPVKASSVFI ADVGLTGELK VCPSIDVRIS EARRMGFKHI
YVPKNIKQES KDLVKLNHIM EVLKHSIEE
//
