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Database: UniProt
Entry: A0A139BVR0_9PROT
LinkDB: A0A139BVR0_9PROT
Original site: A0A139BVR0_9PROT 
ID   A0A139BVR0_9PROT        Unreviewed;       452 AA.
AC   A0A139BVR0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=AWT59_0817 {ECO:0000313|EMBL:KXS33061.1};
OS   Candidatus Gallionella acididurans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS33061.1, ECO:0000313|Proteomes:UP000070578};
RN   [1] {ECO:0000313|EMBL:KXS33061.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33061.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXS33061.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33061.1};
RA   Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA   Pimenov N., Karnachuk O., Ravin N.;
RT   "New uncultured bacterium of the family Gallionellaceae from acid mine
RT   drainage: description and reconstruction of genome based on metagenomic
RT   analysis of microbial community.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC       stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC       DNA, and the ATP-dependent hybridization of homologous single-stranded
CC       DNAs. It interacts with LexA causing its activation and leading to its
CC       autocatalytic cleavage. {ECO:0000256|ARBA:ARBA00025580}.
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:KXS33061.1}.
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DR   EMBL; LSLI01000012; KXS33061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139BVR0; -.
DR   PATRIC; fig|1796491.3.peg.890; -.
DR   Proteomes; UP000070578; 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:0004176; F:ATP-dependent peptidase 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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; IPR008269; Lon_proteolytic.
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; PF05362; Lon_C; 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|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|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070578};
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          67..215
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          351..452
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   MOTIF           252..256
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   452 AA;  48501 MW;  4FB459C4ADF2AC68 CRC64;
     MAKAKTIYSC TECGGQVAKW QGQCPHCEAW NTLVESVAEI APGGKNRFSA LTATGRVQML
     SEVEAAEVPR TPSGIAEFDR VLGGGLVQGA VVLIGGDPGI GKSTLLLQVL AHLSRQQKTL
     YVSGEESAQQ IALRAKRLSL DASSLRLLAE IQLEKIQAAI AQDKPDVVVI DSIQTVYSEQ
     LTSAPGSVAQ VRECAAQLTR VAKSSNITII LVGHVTKEGA LAGPRVLEHI VDTVLYFEGD
     THSSFRLIRA FKNRFGAVNE LGVFAMTEKG LREVSNPSAL FLSQHGEQVA GSCVMVTQEG
     TRPLLVEIQA LLDEAHSPNV RRLSLGLEQN RLAMLLAVLH RHAGIACYDQ DVFINAVGGV
     KITEPGADLA VILAMVSSLR NKPLPAKLVV FGEVGLAGEV RPVQRGQERL REAAKLGFTQ
     AIIPRANAPK QKIPGMEIIA VDRVEQAVDR MR
//
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