RECA_METCL
ID RECA_METCL Reviewed; 342 AA.
AC P24542;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
OS Methylomonas clara.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylothermaceae; Methylothermaceae incertae sedis.
OX NCBI_TaxID=417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31226 / DSM 6330 / FH-B-5460;
RX PubMed=1367275; DOI=10.1007/bf00180631;
RA Ridder R., Marquardt R., Esser K.;
RT "Molecular cloning and characterization of the recA gene of Methylomonas
RT clara and construction of recA deficient mutant.";
RL Appl. Microbiol. Biotechnol. 35:23-31(1991).
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; X59514; CAA42101.1; -; Genomic_DNA.
DR PIR; S18728; S18728.
DR AlphaFoldDB; P24542; -.
DR SMR; P24542; -.
DR PRIDE; P24542; -.
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..342
FT /note="Protein RecA"
FT /id="PRO_0000122754"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 342 AA; 36621 MW; 1C6E777CAADBCFB4 CRC64;
MDDNKSKALA AALSQIEKQF GKGSIMRMGD ADIGEDLQVV STGSLGLDIA LGVGGLPRGR
IIEIYGPESS GKTTLTLSAI AEMQKLGGVA AFIDADDALD PQYASKLGVN VPELLISQPD
TGEQALEIAD MLVRSGSVDI VVVDSVAALT PRAEIEGEMG DSHMGLQARL MSQALRKLTG
NIKRTNTLVI FINQIRMKIG VMFGNPETTT GGNALKFYSS VRLDIRRTGA IKKGDEVIGS
ETKVKVIKNK VAPPFKQAEF DIMYGEGISR LGEIIELGTN LKLVEKSGAW YSYNGEKIGQ
GKENAKEFLR ENPAIAAEIE AKIRDNSNVL ADSMTAARSE DD