ID A0A1S6IT28_9FIRM Unreviewed; 448 AA.
AC A0A1S6IT28;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 08-OCT-2025, entry version 35.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|NCBIfam:TIGR00416};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=B0537_01755 {ECO:0000313|EMBL:AQS57933.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS57933.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS57933.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS57933.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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; CP019698; AQS57933.1; -; Genomic_DNA.
DR RefSeq; WP_077712895.1; NZ_CP019698.1.
DR AlphaFoldDB; A0A1S6IT28; -.
DR STRING; 1833852.B0537_01755; -.
DR KEGG; dfg:B0537_01755; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000189464; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR CDD; cd01121; RadA_SMS_N; 1.
DR FunFam; 3.40.50.300:FF:000050; DNA repair protein RadA; 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; Zn_ribbon_LapB; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Reference proteome {ECO:0000313|Proteomes:UP000189464};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 62..211
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 347..448
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 248..252
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 448 AA; 48165 MW; 7E6C8A647585A382 CRC64;
MRKKTTYACQ ACGHQSARWL GRCPGCGQWN TMVEERTEAP VKTVRGLSGS GPVPVTDIVT
TSEERYPTGL SELDRVLGGG VVPGSLVLVG GDPGIGKSTL LLQVAAALAA RIGKVLYVSG
EESAQQIKMR AERIGALHSH LLLMSETDMS GIEKVIQESK PSAVILDSIQ TVYYPEVSSA
PGSVAQVREC TAILMRLAKG TGIPVFVVGH VTKEGTLAGP RVLEHMVDTV LYFEGERHQA
YRILRTVKNR FGSTNELGIF EMRGQGLVEI LNPSELFMNQ RPEAVPGSAI IPSLEGSRPL
LVEIQALVCP TAFGTPRRMT SGLDYNRVAL IMAVLERRVG LRLSNYDAYV SAVGGVKLDE
PAADLAVALA IASSFKERPL QNHLVLVGEV GLTGEIRPVS GMDKRLHEAA KLGFKLCIGP
ARERQSLDII EYSGVQSIQE AVEAAMGR
//
