ID A0A0F6A994_9GAMM Unreviewed; 456 AA.
AC A0A0F6A994;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=N479_16850 {ECO:0000313|EMBL:KKE82723.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE82723.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE82723.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE82723.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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}.
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:KKE82723.1}.
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DR EMBL; AUXW01000157; KKE82723.1; -; Genomic_DNA.
DR RefSeq; WP_039611945.1; NZ_AUXW01000157.1.
DR AlphaFoldDB; A0A0F6A994; -.
DR PATRIC; fig|1129367.4.peg.3349; -.
DR Proteomes; UP000033434; 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 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|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|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..219
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 355..456
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 256..260
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 456 AA; 49034 MW; 36F3845F37A5D4FE CRC64;
MGKKKTAFVC SDCGAEFARW QGQCSECKAW NTVTEFRVPS VKAAPRSAGT TGYAGVVEAK
IQTLDEVNLE SLPRFSTGFK EFDRVLGGGV VPGSAILIGG EPGAGKSTLL LQTMCLLAQS
MPTLYVTGEE SLQQVAMRAK RLGLPTDKLK TLAETNVETI CQLALREKPA IMVIDSIQVM
HMTDVQSAPG SVSQVRESAA YLTRFAKQNQ VAIIMVGHVT KDGTLAGPKV LEHCIDCSIL
LEGSSDSRFR TLRGNKNRFG AVNELGVFAM TGQGLKEVNN PSAIFLNRGE EQTPGSLVMV
IWEGTRPLLV EVQALVDYSQ LANPRRVTVG LEQNRLAMLL AVLHRHGGLQ VADQDVFVNV
VGGVKVNETS ADLALITALV SSFKNYALDK QLVVFGEVGL GGEIRPVPSG QERLREAAKH
GFKRAIVPVA NKPKEDIEGM EVIGVSSLND ALQALF
//