RADA_SALTY
ID RADA_SALTY Reviewed; 460 AA.
AC P24517;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498};
DE AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; OrderedLocusNames=STM4579;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-460.
RC STRAIN=LT2;
RX PubMed=2198247; DOI=10.1128/jb.172.8.4187-4196.1990;
RA Foster J.W., Park Y.K., Penfound T., Fenger T., Spector M.P.;
RT "Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence
RT analysis of the bifunctional nadR regulator and the nadA-pnuC operon.";
RL J. Bacteriol. 172:4187-4196(1990).
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:0000255|HAMAP-Rule:MF_01498}.
CC -!- DOMAIN: Has a putative N-terminal zinc-finger, a middle region with
CC homology to RecA with ATPase motifs including the RadA KNRFG motif,
CC while the C-terminus is homologous to Lon protease. {ECO:0000255|HAMAP-
CC Rule:MF_01498}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M85181; Type=Frameshift;
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DR EMBL; AE006468; AAL23394.1; -; Genomic_DNA.
DR EMBL; M85181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A37753; A37753.
DR RefSeq; NP_463435.1; NC_003197.2.
DR RefSeq; WP_001029709.1; NC_003197.2.
DR AlphaFoldDB; P24517; -.
DR SMR; P24517; -.
DR STRING; 99287.STM4579; -.
DR MEROPS; S16.A04; -.
DR PaxDb; P24517; -.
DR PRIDE; P24517; -.
DR EnsemblBacteria; AAL23394; AAL23394; STM4579.
DR GeneID; 1256105; -.
DR KEGG; stm:STM4579; -.
DR PATRIC; fig|99287.12.peg.4822; -.
DR HOGENOM; CLU_018264_0_1_6; -.
DR OMA; FELMRLA; -.
DR PhylomeDB; P24517; -.
DR BioCyc; SENT99287:STM4579-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR CDD; cd01121; Sms; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00416; sms; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..460
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187937"
FT ZN_FING 11..28
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 357..460
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 258..262
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 460 AA; 49426 MW; AB66140AB2555DB8 CRC64;
MAKAPKRAFV CNECGADYPR WQGQCSACHA WNTITEVRLA ASPTVARNER LSGYAGSAGV
SKVQKLSDIS LEELPRFSTG FKEFDRVLGG GVVPGSAILI GGNPGAGKST LLLQTLCKLA
EQMKTLYVTG EESLQQVAMR AHRLGLPTAN LNMLSETSIE QICLIAEEEQ PKLMVIDSIQ
VMHMADIQSS PGSVAQVRET AAYLTRFAKT RGVAIVMVGH VTKDGSLAGP KVLEHCIDCS
VLLDGDADSR FRTLRSHKNR FGAVNELGVF AMTEQGLREV SNPSAIFLSR GDEVTSGSSV
MVVWEGTRPL LVEIQALVDH SMMANPRRVA VGLEQNRLAI LLAVLHRHGG LQMSDQDVFV
NVVGGVKVTE TSADLALLLA MVSSLRDRPL PQDLVVFGEV GLAGEIRPVP SGQERISEAA
KHGFRRAIVP AANVPKKPPE GMLVFGVKKL ADALSVFDDL
