RADA_LISMO
ID RADA_LISMO Reviewed; 457 AA.
AC Q48761; O86063;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
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}; Synonyms=sarII, sms;
GN OrderedLocusNames=lmo0233;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=8885268; DOI=10.1046/j.1365-2958.1996.641432.x;
RA Rouquette C., Ripio M.T., Pellegrini E., Bolla J.-M., Tascon R.I.,
RA Vazquez-Boland J.A., Berche P.;
RT "Identification of a ClpC ATPase required for stress tolerance and in vivo
RT survival of Listeria monocytogenes.";
RL Mol. Microbiol. 21:977-987(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2175 / Serovar 4b;
RA Truong T.K., Kathariou S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; U40604; AAC44447.1; -; Genomic_DNA.
DR EMBL; AF083254; AAC33293.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00760.1; -; Genomic_DNA.
DR PIR; AB1104; AB1104.
DR RefSeq; NP_463764.1; NC_003210.1.
DR RefSeq; WP_010989380.1; NZ_CP023861.1.
DR AlphaFoldDB; Q48761; -.
DR SMR; Q48761; -.
DR STRING; 169963.lmo0233; -.
DR MEROPS; S16.A04; -.
DR PaxDb; Q48761; -.
DR EnsemblBacteria; CAD00760; CAD00760; CAD00760.
DR GeneID; 987204; -.
DR KEGG; lmo:lmo0233; -.
DR PATRIC; fig|169963.11.peg.241; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_9; -.
DR OMA; FELMRLA; -.
DR PhylomeDB; Q48761; -.
DR BioCyc; LMON169963:LMO0233-MON; -.
DR Proteomes; UP000000817; 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..457
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187931"
FT ZN_FING 12..29
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 353..457
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 254..258
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT CONFLICT 37
FT /note="E -> K (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="E -> Q (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> S (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> S (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="Q -> R (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> P (in Ref. 1; AAC44447 and 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="T -> S (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..227
FT /note="PR -> AP (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="H -> P (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="R -> P (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="TN -> PI (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="G -> S (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="G -> R (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..317
FT /note="SMEGTRPVLVEIQALVSPT -> LWKNSPRPCGNTSACFAN (in Ref.
FT 1; AAC44447)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="R -> C (in Ref. 2; AAC33293)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="R -> S (in Ref. 1; AAC44447)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="F -> S (in Ref. 1; AAC44447)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..455
FT /note="Missing (in Ref. 1; AAC44447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49982 MW; 8F7386FC40131359 CRC64;
MAKAKRTTKF VCQACGYESA KWMGKCPNCN EWNQMVEALE PSKKSRSAFN HTGEPSKATP
ITQIASETEK RVETNMPELN RVLGGGVVPG SMVLVGGDPG IGKSTLLLQV SAQLTLTNKK
VLYISGEESI KQTKLRAERL QVSGDNLYVY AETNLEAVQE TIDFVKPDFV VIDSIQTVYH
SDVTSAAGSV SQVRECTATL MRIAKMQNIA IFIVGHVTKE GAIAGPRLLE HMVDTVLYFE
GERHHAYRIL RAVKNRFGST NEMGIFEMRD VGLVEVANPS EVFLEERLEG ASGSTVVASM
EGTRPVLVEI QALVSPTMFG NAKRMATGID YNKVSLIMAV LEKRVGLMLQ NQDAYLKAAG
GVKLDEPAVD LAVAVSVASS YRDKPTRSTD CFIGELGLTG EIRRVARIEQ RVQEAAKLGF
KRIFIPKNNE GNWKIPKDVQ VVGVETIGEA LKKALPD
