ID Q938U3_BORGA Unreviewed; 53 AA. AC Q938U3; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 16-DEC-2008, entry version 37. DE RecName: Full=Protein recA; DE Flags: Fragment; GN Name=recA; OS Borrelia garinii. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=29519; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=387 CSF; RA Makinen J., Vuorinen I., Marjamaki M., He Q., Suhonen J., RA Viljanen M.K.; RT "Prevalence of Borrelia burgdorferi sensu lato and Granulocytic RT Ehrlichiae in Ixodes ricinus Ticks from Turku and Turku archipelago in RT Finland and Vormsi Island in Estonia."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=20047; RX PubMed=16585709; DOI=10.1099/ijs.0.64050-0; RA Richter D., Postic D., Sertour N., Livey I., Matuschka F.R., RA Baranton G.; RT "Delineation of Borrelia burgdorferi sensu lato species by multilocus RT sequence analysis and confirmation of the delineation of Borrelia RT spielmanii sp. nov."; RL Int. J. Syst. Evol. Microbiol. 56:873-881(2006). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IP89, VS102, P/Bi, and VSPB; RX PubMed=15336411; DOI=10.1016/j.femsle.2004.07.025; RA Casati S., Bernasconi M.V., Gern L., Piffaretti J.C.; RT "Diversity within Borrelia burgdorferi sensu lato genospecies in RT Switzerland by recA gene sequence."; RL FEMS Microbiol. Lett. 238:115-123(2004). CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of CC single-stranded DNA, the ATP-dependent uptake of single-stranded CC DNA by duplex DNA, and the ATP-dependent hybridization of CC homologous single-stranded DNAs. It interacts with lexA causing CC its activation and leading to its autocatalytic cleavage (By CC similarity). CC -!- SIMILARITY: Belongs to the recA family. 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; AY048584; AAL05429.1; -; Genomic_DNA. DR EMBL; AY586372; AAT37918.1; -; Genomic_DNA. DR EMBL; AY586373; AAT37919.1; -; Genomic_DNA. DR EMBL; AY586374; AAT37920.1; -; Genomic_DNA. DR EMBL; AY586376; AAT37922.1; -; Genomic_DNA. DR EMBL; DQ111059; AAZ83619.1; -; Genomic_DNA. DR HSSP; Q59560; 1UBE. DR SMR; Q938U3; 1-53. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW. DR InterPro; IPR013765; RecA. DR InterPro; IPR001553; RecA_bac. DR PANTHER; PTHR22942:SF1; RecA; 1. DR Pfam; PF00154; RecA; 1. DR PRINTS; PR00142; RECA. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding; DNA damage; DNA recombination; DNA-binding; KW Nucleotide-binding. FT NON_TER 1 1 FT NON_TER 53 53 SQ SEQUENCE 53 AA; 5600 MW; 11FCBECD7F3EDCD8 CRC64; IGGYPRGRII EIFGPESSGK TTLTLQAIAE VQKEGGIAAF IDAEHALDPV YAK //