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Database: UniProt
Entry: Q092E9_STIAD
LinkDB: Q092E9_STIAD
Original site: Q092E9_STIAD 
ID   Q092E9_STIAD            Unreviewed;       453 AA.
AC   Q092E9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
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   ECO:0000313|EMBL:EAU66595.1};
GN   OrderedLocusNames=STAUR_1881 {ECO:0000313|EMBL:ADO69685.1};
GN   ORFNames=STIAU_3597 {ECO:0000313|EMBL:EAU66595.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU66595.1, ECO:0000313|Proteomes:UP000032702};
RN   [1] {ECO:0000313|EMBL:EAU66595.1, ECO:0000313|Proteomes:UP000032702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU66595.1,
RC   ECO:0000313|Proteomes:UP000032702};
RA   Nierman W.C.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO69685.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69685.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO69685.1; -; Genomic_DNA.
DR   EMBL; AAMD01000051; EAU66595.1; -; Genomic_DNA.
DR   RefSeq; WP_002613827.1; NZ_AAMD01000051.1.
DR   STRING; 378806.STAUR_1881; -.
DR   MEROPS; S16.A04; -.
DR   KEGG; sur:STAUR_1881; -.
DR   PATRIC; fig|378806.16.peg.5763; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_7; -.
DR   OMA; FELMRLA; -.
DR   OrthoDB; 9803906at2; -.
DR   Proteomes; UP000001351; Chromosome.
DR   Proteomes; UP000032702; 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   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..453
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   453 AA;  47873 MW;  D0C8B0E4877F7CDD CRC64;
     MAKAKTHYSC QACGYQTAKW LGKCPDCGAW SSLLEESEAK PDEKRPAWGA SGGSTKPVLL
     KDVSGEVEAR RRTGIAEFDR VLGGGVVGGS LVLLGGDPGI GKSTLLLAAL DRLARHGPVL
     YVSGEESLRQ TKMRAERLRV EGEAIHLFAE TDADRVLSAA EALKPMALVV DSIQTMYLPE
     LGSAPGSITQ VREVAGRLMA YAKRTGVPTF IVGHVTKEGS IAGPRVLEHM VDTVLYFEGE
     RGHPFRILRA HKNRFGSTNE IGVFEMKGLG LVEVPDPSAL FLAERPAGKA GSVVTSTLNG
     TRPLLVEVQA LVAPTGYGTA RRTAIGVDGN RVALLAAVLE KKEDIPLVGC DLFVNVAGGM
     QLSEPACDLA VCAALVSSLQ NRPLDPHTLV LGEVGLAGEV RAVGQVEPRL AEASKMGFQR
     VVLPSGSARR LEAAKLKVVG VETLGEALSA MFD
//
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