ID E6NQA1_HELPQ Unreviewed; 448 AA.
AC E6NQA1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:BAJ59317.1};
GN OrderedLocusNames=HPF57_0243 {ECO:0000313|EMBL:BAJ59317.1};
OS Helicobacter pylori (strain F57).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ59317.1, ECO:0000313|Proteomes:UP000008082};
RN [1] {ECO:0000313|EMBL:BAJ59317.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59317.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Evolution in an oncogenic bacterial species with extreme genome
RT plasticity: Helicobacter pylori East Asian genomes.";
RL BMC Microbiol. 11:104-104(2011).
RN [2] {ECO:0000313|EMBL:BAJ59317.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59317.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Birth and death of genes linked to chromosomal inversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(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; AP011945; BAJ59317.1; -; Genomic_DNA.
DR RefSeq; WP_014535543.1; NC_017367.1.
DR AlphaFoldDB; E6NQA1; -.
DR KEGG; hex:HPF57_0243; -.
DR PATRIC; fig|866346.4.peg.265; -.
DR HOGENOM; CLU_018264_0_1_7; -.
DR Proteomes; UP000008082; 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|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..216
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 351..448
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 253..257
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 448 AA; 49478 MW; 967024E8A9A90871 CRC64;
MAKKTSLFEC QHCGFTSPKW LGKCVQCNAW ESFIELNQTQ KEVLNALKNP LPKAQKSVSI
AEIEHEEVIK FSSTQSELDI VLGGGIAKGG LYLVGGSPGV GKSTLLLKVA SGLAKNQQKV
LYVSGEESLS QIKMRATRLD CIEKELYLLN EINWPVIKAN IESENYFACV IDSIQTLYLP
EISSAPGSIS QVREITFELM RLAKTRNIAV FIIGHITKEG SIAGPRVLEH MVDSVLYFEG
DPSRELRILR SFKNRFGPTS EIGLFEMKEQ GLVSAKEASS LFFSKEEPME GSAITITLEG
SRALILEIQA LVSECSFGAP KRLANGFDTN RLNMLIALLE KKLEIPLNRH DVFINVSGGI
KISEPACDLA VIASILSSFK NRKIDNKTAF LGEVSLNGRI LEAPNLNARL KEMENYGFLK
AILPKKPSQK TSIKCYEANA VGKIVEWM
//
