ID A0A077AXW8_9PROT Unreviewed; 460 AA.
AC A0A077AXW8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=ID47_06525 {ECO:0000313|EMBL:AIK96473.1};
OS Candidatus Paracaedibacter acanthamoebae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales;
OC Candidatus Paracaedibacteraceae; Paracaedibacter.
OX NCBI_TaxID=91604 {ECO:0000313|EMBL:AIK96473.1, ECO:0000313|Proteomes:UP000028926};
RN [1] {ECO:0000313|EMBL:AIK96473.1, ECO:0000313|Proteomes:UP000028926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRA3 {ECO:0000313|EMBL:AIK96473.1};
RA Wang Z., Wu M.;
RT "Comparative genomic insights into amoeba endosymbionts belonging to the
RT families of Holosporaceae and Candidatus Midichloriaceae within
RT Rickettsiales.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CP008941; AIK96473.1; -; Genomic_DNA.
DR RefSeq; WP_038464911.1; NZ_CP008941.1.
DR AlphaFoldDB; A0A077AXW8; -.
DR STRING; 91604.ID47_06525; -.
DR KEGG; paca:ID47_06525; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_5; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000028926; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000028926};
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 63..214
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 350..460
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 251..255
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 460 AA; 49354 MW; 6424B03A37722099 CRC64;
MAKISLKYVC QDCGTVHSKW GGKCEGCSAW NTLQEEAMQV SKKPVTAKRT NLEFVSIESE
TIETDRLLTH MAEFDRVCGG GLVPGGVLLV GGDPGIGKST LLLQVVSKFS QNYSCAYVSG
EEAVGQVRMR AKRLGVANSD NLHLASATSV SDILAALDNL ENPIKLLIID SIQTMTNADV
DSAPGTVSQV RVCTQELIAY AKSKGVVVIL VGHVTKEGVI AGPRVLEHMV DTVLYFEGER
NYHYRILRSV KNRFGPTDEI GVFEMTDLGL QEVPNPSALF LNQHDYPVSG SAIFAGIEGT
RPILIEVQAL VAPSHLATPR RTSVGWDSNR LAMIIAVLES RCGLSFANKD VFLNVAGGLK
ISEPASDLAV AAALASTLSN TPTPVKSVFF GEIGLSGEVR AVSQSDLRLK EASKLGFAVG
FCGKLSKGGQ SSDLAITPLN YLIEMMDIFK NPHHSKVKFV
//
