ID RECA_LACPE Reviewed; 378 AA. AC Q6KCK3; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-FEB-2021, entry version 71. 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 Lactobacillus pentosus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=1589; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026; RX PubMed=16014493; DOI=10.1099/ijs.0.63333-0; RA Bringel F., Castioni A., Olukoya D.K., Felis G.E., Torriani S., RA Dellaglio F.; RT "Lactobacillus plantarum subsp. argentoratensis subsp. nov., isolated from RT vegetable matrices."; RL Int. J. Syst. Evol. Microbiol. 55:1629-1634(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ621666; CAF21791.1; -; Genomic_DNA. DR RefSeq; WP_050339350.1; NZ_RDCL01000052.1. DR SMR; Q6KCK3; -. DR PRIDE; Q6KCK3; -. DR GeneID; 49394474; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0008094; F:DNA-dependent ATPase activity; 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; 3.30.250.10; -; 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..378 FT /note="Protein RecA" FT /id="PRO_0000122735" FT NP_BIND 65..72 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268" SQ SEQUENCE 378 AA; 40690 MW; 0CF98BB77F20ADCF CRC64; MADARKAALD TALKKIEKNF GKGAIMRMGD AAQTTISTIS SGSLALDDAL GVGGYPRGRI VEIYGPESSG KTTVALHAVA EVQKQGGTAA YIDAENALDP VYAEHLGVNI DDLLLSQPDT GEQGLEIADA LVSSGAVDIL VVDSVAALVP RAEIEGEMGD AHVGLQARLM SQALRKLSGT LNKTKTIALF INQIREKVGV MFGNPETTPG GRALKFYATI RLEVRRAEQI KEGTNIIGNR VRIKVVKNKV APPFKRAEVD IMYGQGISQT GEIVDMAAEK DIVKKSGSWY SYGDDRIGQG RENAKKYLDE HPDVMAEIRQ KVRDAYGMDQ TGEEDDQADD KSKDKATKPS DKSQAQAKPK KPVATETSLD LDDSKTDK //