ID A0A2Z5YY54_9SPHN Unreviewed; 455 AA.
AC A0A2Z5YY54;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AEB_P2243 {ECO:0000313|EMBL:BBC73111.1};
OS Altererythrobacter sp. B11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=2060312 {ECO:0000313|EMBL:BBC73111.1, ECO:0000313|Proteomes:UP000263119};
RN [1] {ECO:0000313|EMBL:BBC73111.1, ECO:0000313|Proteomes:UP000263119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11 {ECO:0000313|EMBL:BBC73111.1,
RC ECO:0000313|Proteomes:UP000263119};
RA Maeda A.H., Nishi S., Ishii S., Shimane Y., Kobayashi H., Ichikawa J.,
RA Kurosawa K., Arai W., Takami H., Ohta Y.;
RT "Complete Genome Sequence of Altererythrobacter sp. Strain B11, an Aromatic
RT Monomer-Degrading Bacterium, Isolated from Deep-Sea Sediment under the
RT Seabed off Kashima, Japan.";
RL Genome Announc. 6:e00200-18(2018).
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; AP018498; BBC73111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5YY54; -.
DR KEGG; alb:AEB_P2243; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000263119; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000263119};
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 66..216
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 353..455
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 253..257
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 455 AA; 47943 MW; 7315A9E282FB4631 CRC64;
MAKPKRRYVC ADCGSVSSRW QGQCADCGQW NTLSEEAPET TFSARHDLSG GGRRLAFEPL
DAPAEVLTRR STGLEEFDRA LGGGIVPGSA ILMGGEPGIG KSTLLLQAAA AVARSGAEAV
YVSGEEATGQ VRMRARRLGL SDSPLKLAAA TSVRDILTTL HAGPQPALLI VDSIQTMHSD
VIEGAPGTVS QVRASAFELI RYAKENGVAL VLVGHVTKDG TIAGPRVLEH MVDVVMSFEG
ERSHQYRILR ALKNRFGAVD EIGVFAMEGQ GLAEVSNPSM LFLSGREQPV AGSSVFPALE
GTRPVLIEVQ ALIVRLQSGA TPRRAVVGWD SGRLAMLLAV LESRCGLNFS SAEVYLNVAG
GYRLTDPAAD LAVAAALVSA LADKPLPLRS VWFGEVSLSG EIRPVAHSGL RLREAAKLGF
DRGAGPEDAG KGVPALRYSG MATLPKLVDR IMGGE
//