ID A0A101HTT1_9FIRM Unreviewed; 363 AA.
AC A0A101HTT1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
DE Flags: Fragment;
GN ORFNames=XD97_0368 {ECO:0000313|EMBL:KUK82694.1};
OS Pelotomaculum thermopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=110500 {ECO:0000313|EMBL:KUK82694.1, ECO:0000313|Proteomes:UP000054705};
RN [1] {ECO:0000313|Proteomes:UP000054705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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 -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {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:KUK82694.1}.
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DR EMBL; LGGS01000073; KUK82694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HTT1; -.
DR PATRIC; fig|110500.4.peg.635; -.
DR Proteomes; UP000054705; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 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 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|RuleBase:RU003555};
KW DNA damage {ECO:0000256|RuleBase:RU003555};
KW DNA repair {ECO:0000256|RuleBase:RU003555};
KW DNA-binding {ECO:0000256|RuleBase:RU003555};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|RuleBase:RU003555};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003555};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 1..124
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK82694.1"
SQ SEQUENCE 363 AA; 38465 MW; 53E1F1E24B43D6D4 CRC64;
LVGGDPGIGK STLLLQVLES LARKGLKVLY ITGEESARQI KLRGKRVGAS SRDLLVMVEI
ALENILKQIK ATSPETVVID SIQTIYSSAL SSAPGSVGQV REAAERLIVE AKKSGIPIFL
IGHVTKDGSI AGPKVLEHMV DTVLYLEGDR HHCFRILRGV KNRFGSTNEI GIFEMRNHGL
TEVTNPAAVF LTRRSRQDVP GSAITAGLEG TRPMLVEIQA LVSPAAYGVP RRMTAGVEHN
RVALIVAVLE KRVGLNFAQH DIYVNAVGGA KVDEPAADLA IALALASSLK DVAVDARLVC
AGEIGLTGEL RPVTGAEKRV NEAFKLGFTQ FMLSGQSPAA VLNKTGVSAA DTLAGALELA
LML
//
