RECA_CORGL
ID RECA_CORGL Reviewed; 376 AA.
AC P42442;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
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};
GN OrderedLocusNames=Cgl1955, cg2141;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Kerins S.M., Fitzpatrick R., O'Donohue M., Dunican L.K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=7841463; DOI=10.3109/10425179409010189;
RA Billman-Jacobe H.;
RT "Nucleotide sequence of a recA gene from Corynebacterium glutamicum.";
RL DNA Seq. 4:403-404(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-200.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=7765733; DOI=10.1007/bf00173923;
RA Fitzpatrick R., O'Donohue M., Joy J., Heery D.M., Dunican L.K.;
RT "Construction and characterization of recA mutant strains of
RT Corynebacterium glutamicum and Brevibacterium lactofermentum.";
RL Appl. Microbiol. Biotechnol. 42:575-580(1994).
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.
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; U14965; AAD12743.1; -; Genomic_DNA.
DR EMBL; X77384; CAA54563.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99348.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20296.1; -; Genomic_DNA.
DR EMBL; X75085; CAA52977.1; -; Genomic_DNA.
DR PIR; I40728; I40728.
DR RefSeq; NP_601162.1; NC_003450.3.
DR RefSeq; WP_003857444.1; NC_006958.1.
DR AlphaFoldDB; P42442; -.
DR SMR; P42442; -.
DR STRING; 196627.cg2141; -.
DR GeneID; 58308646; -.
DR KEGG; cgb:cg2141; -.
DR KEGG; cgl:Cgl1955; -.
DR PATRIC; fig|196627.13.peg.1893; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_11; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000000582; 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; EXP:CollecTF.
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; Reference proteome; SOS response.
FT CHAIN 1..376
FT /note="Protein RecA"
FT /id="PRO_0000122696"
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"
FT CONFLICT 2
FT /note="A -> H (in Ref. 2; CAA54563)"
FT /evidence="ECO:0000305"
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
