RECA_CORGB
ID RECA_CORGB Reviewed; 376 AA.
AC A4QEW3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=cgR_1785;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage. {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; AP009044; BAF54779.1; -; Genomic_DNA.
DR RefSeq; WP_003857444.1; NC_009342.1.
DR AlphaFoldDB; A4QEW3; -.
DR SMR; A4QEW3; -.
DR EnsemblBacteria; BAF54779; BAF54779; cgR_1785.
DR GeneID; 58308646; -.
DR KEGG; cgt:cgR_1785; -.
DR HOGENOM; CLU_040469_3_2_11; -.
DR OMA; DYGEQAL; -.
DR PhylomeDB; A4QEW3; -.
DR Proteomes; UP000006698; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; SOS response.
FT CHAIN 1..376
FT /note="Protein RecA"
FT /id="PRO_1000047906"
FT REGION 355..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 376 AA; 40228 MW; 5535924F18549D5C CRC64;
MAPKKTATKA TAAKGNDRQK ALDAALALIE KDFGKGAVMR LGDENRPPIQ TISSGNTAID
IALGIGGFPR GRIVEVYGPE SSGKTTVALH AIAQAQKAGG IAAFIDAEHA LDPDYARKLG
VDTDALLVSQ PDTGEQALEI ADMLVRSGAI DIIVIDSVAA LTPKAEIEGE MGDSHVGLQA
RLMSQALRKM TGALYNSGTT AIFINQLREK IGVMFGSPET TTGGKALKFY ASVRCDIRRI
QTLKDGQDAI GNRTRLKVVK NKVSPPFKIA EFDIMYGEGI SRESSVIDLA VDNGIVKKSG
SWFTYEGEQL GQGKEKVRLS LKENPELTDE LEDKIFKKLG VGKYAAASDE LTDDPVELVP
NVDFDDEADT EADAED