ID A0A2P4UKK3_9ACTN Unreviewed; 475 AA.
AC A0A2P4UKK3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BTM25_42350 {ECO:0000313|EMBL:POM25587.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM25587.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM25587.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM25587.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM25587.1}.
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DR EMBL; MTBP01000002; POM25587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UKK3; -.
DR Proteomes; UP000242367; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000242367};
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 68..222
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 358..475
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 259..263
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 475 AA; 49341 MW; 0673154F621ECCCF CRC64;
MAKAKTARQA SYRCSECGWQ TSKWVGRCGE CQAWGTVLEA AGASPARVVA AGAVSAPARP
IGQVDVRSAR TRPTGLDELD RVLGGGIVPG AVLLLAGEPG IGKSTLLLEV AALASGAGEG
AEAQPVLYVT GEESAQQVRL RADRIGAVTD TLYLAAETEL SAVLGHVDTV SPALLVVDSI
QTIGTAEADG APGGVTQIRE VAANLIRVAK ERGIPVVLVG HVTKEGAIAG PRLLEHLVDV
VLYFEGDRHS RLRMIRAVKN RYGPTDELGC FDLSEVGIVG VADPSGLFLT RREEPVPGTC
VTVTLEGRRP LVAEVQALVA KSHLPAPRRA SSGLETSRVA MVLAVLAQRC KISMHEQDVY
VSTVGGVRLA ETSVDLALAL AVAGSTVEQA LSGGLIAVGE VGLAGEVRVV PGVPRRLAEA
ARLGFKYAVV PRGSLDLGDG SPLKRADPQL TSHEGMKVME VDSLTQALQV AFTAP
//