RADA_CAMJE
ID RADA_CAMJE Reviewed; 446 AA.
AC Q9PN90; Q0P951;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=Cj1205c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
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DR EMBL; AL111168; CAL35320.1; -; Genomic_DNA.
DR PIR; G81326; G81326.
DR RefSeq; WP_002858434.1; NC_002163.1.
DR RefSeq; YP_002344596.1; NC_002163.1.
DR AlphaFoldDB; Q9PN90; -.
DR SMR; Q9PN90; -.
DR IntAct; Q9PN90; 4.
DR STRING; 192222.Cj1205c; -.
DR MEROPS; S16.A04; -.
DR PaxDb; Q9PN90; -.
DR PRIDE; Q9PN90; -.
DR EnsemblBacteria; CAL35320; CAL35320; Cj1205c.
DR GeneID; 905495; -.
DR KEGG; cje:Cj1205c; -.
DR PATRIC; fig|192222.6.peg.1186; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_7; -.
DR OMA; FELMRLA; -.
DR Proteomes; UP000000799; 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; IEA:UniProtKB-UniRule.
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..446
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187922"
FT ZN_FING 10..27
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 349..446
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 253..257
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 446 AA; 49025 MW; D3B79419206D3F1F CRC64;
MAKNKALFEC QACGNQQSKW LGKCPDCGAW DSFVELKAEQ IKVLKELAQV SMKTSEAVCI
EDVELEHFTR YSTDDNELDL VLGGGLVEGS LVLIGGSPGV GKSTLLLKIA SNLAKQGKKV
LYVSGEESKA QIKLRADRLE ANTPNLFLLT ELCLENILEE LHKKDYSILI VDSIQTLYSN
KITSAAGSIT QVREITFELM RVSKAYNIST FIIGHITKEG AIAGPRVLEH MVDVVLYFEG
DATKEIRLLR GFKNRFGGTN EVGIFEMTAK GLISAKDLAN RFFTRGKAIS GSALGVVMEG
SRALVLEVQA LVCESSYPKR SATGYEKNRL DMLLALLERK LEIPLGHYDV FVNISGGVKV
SETAADLAVV AAIISSFKNR PLSKDSIFIG ELSLNGEIRE VFSLDTRLKE AKMQKFKNAI
VPSKPLEDIG LKCFVAKELS QVLEWM
