ID A0A1Y1CIZ6_9BACT Unreviewed; 458 AA.
AC A0A1Y1CIZ6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=ALGA_1936 {ECO:0000313|EMBL:BAX80295.1};
OS Labilibaculum antarcticum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Labilibaculum.
OX NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX80295.1, ECO:0000313|Proteomes:UP000218267};
RN [1] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:BAX80295.1, ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|EMBL:BAX80295.1,
RC ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 39:1-2(2018).
RN [3] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL Antonie Van Leeuwenhoek 113:349-355(2020).
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; AP018042; BAX80295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1CIZ6; -.
DR KEGG; mbas:ALGA_1936; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000218267; Chromosome.
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 71..218
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..458
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 255..259
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 458 AA; 49812 MW; 0E9F350DB28E2E82 CRC64;
MATKAKTKSA WFCQTCGVES AKWVGKCPSC GEWNSFVEEV VVKSSPSQII GSNGQGKKNK
PQKISEISSS EASRFDTKNE ELNRVLGGGL VPGSLILIGG EPGIGKSTLA LQIALNLKNY
TTLYVSGEES AQQIKLRGNR INSDNENCLI VSETSMENIF SHVKNTSPDI IVIDSIQTLA
TESIEAGPGS VSQIRECTSQ LLRFAKESST PVILIGHITK DGNLAGPKIL EHMVDTVLQF
EGDQNHMYRI LRSTKNRFGS TSEMGIYEMQ HNGLREVSNP SELLLSQDDE SLSGVTISAS
IEGMRPFLIE TQALVSSAAY GTPQRSSTGF DLRRLNMLLA VLEKRAGFKL STKDVFLNIA
GGIKVNDPAI DLAVILAVLS SSTDISIPKE VCFSGEIGLS GEIRPVSRID QRISEAEKLG
FKQIFIPKHN SKGLDTSKFK IKIHLVSKVG EVFQTLFR
//
