RECA_MYCPN
ID RECA_MYCPN Reviewed; 336 AA.
AC P78014;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=MPN_490;
GN ORFNames=MP352;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 -!- INTERACTION:
CC P78014; P75080: polC; NbExp=3; IntAct=EBI-2258718, EBI-2258713;
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; U00089; AAB96000.1; -; Genomic_DNA.
DR PIR; S73678; S73678.
DR RefSeq; NP_110178.1; NC_000912.1.
DR RefSeq; WP_010874846.1; NC_000912.1.
DR AlphaFoldDB; P78014; -.
DR SMR; P78014; -.
DR IntAct; P78014; 2.
DR STRING; 272634.MPN_490; -.
DR PRIDE; P78014; -.
DR EnsemblBacteria; AAB96000; AAB96000; MPN_490.
DR GeneID; 66608837; -.
DR KEGG; mpn:MPN_490; -.
DR PATRIC; fig|272634.6.peg.530; -.
DR HOGENOM; CLU_040469_1_2_14; -.
DR OMA; DYGEQAL; -.
DR BioCyc; MPNE272634:G1GJ3-805-MON; -.
DR Proteomes; UP000000808; 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 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..336
FT /note="Protein RecA"
FT /id="PRO_0000122765"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 336 AA; 36918 MW; EA580D4A7657EB4D CRC64;
MVQKEMINKK ISQDNSFIQN NNLADFDFLD AKKNSEIKTV STGSLHLDEA LGTGGLPLGR
IVELYGNESS GKTTVALHAV ASFQKAGKVA CYIDAEGALD LSYAKAIGID LGKLLVAHPK
HGENAFALME SLIKTNKVAL IVVDSVAALI PKQELEGNMD DQTIGLHARM MSKGLRRVQS
LLPESDTCLL FINQLREKPG VMFGNGEVTT GGRALKFYAS MRMEAKRSEL LKDRFGNYVG
IKSKLTVSKN KVARPFGVAF LEIMFNRGIV YEHEVIELAL KHNVVVRSDN AYSFKSQNIA
IGKEKLFSVL AEKPELFEQI KQLTIKQIHS PPPPAS
