RECA_LEGPN
ID RECA_LEGPN Reviewed; 348 AA.
AC Q05358; Q9AKW1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2121588; DOI=10.1111/j.1574-6968.1990.tb13983.x;
RA Zhao X., Dreyfus L.A.;
RT "Expression and nucleotide sequence analysis of the Legionella pneumophila
RT recA gene.";
RL FEMS Microbiol. Lett. 58:227-231(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43109 / NCTC 12008 / RC1 / Olda / Serogroup 1;
RX PubMed=11251842; DOI=10.1111/j.1365-2958.2001.02314.x;
RA Lueneberg E., Mayer B., Daryab N., Kooistra O., Zaehringer U., Rohde M.,
RA Swanson J., Frosch M.;
RT "Chromosomal insertion and excision of a 30 kb unstable genetic element is
RT responsible for phase variation of lipopolysaccharide and other virulence
RT determinants in Legionella pneumophila.";
RL Mol. Microbiol. 39:1259-1271(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA39098.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X55453; CAA39097.1; -; Genomic_DNA.
DR EMBL; X55453; CAA39098.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ277756; CAC33484.1; -; Genomic_DNA.
DR PIR; A60989; A60989.
DR RefSeq; WP_010947527.1; NZ_UGOV01000002.1.
DR AlphaFoldDB; Q05358; -.
DR SMR; Q05358; -.
DR STRING; 91892.BIZ52_08625; -.
DR GeneID; 66490933; -.
DR eggNOG; COG0468; Bacteria.
DR OrthoDB; 1080436at2; -.
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..348
FT /note="Protein RecA"
FT /id="PRO_0000122740"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 13
FT /note="V -> L (in Ref. 2; CAC33484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 37935 MW; 1FB0B182FC41A035 CRC64;
MEENKQKALS AAVSQIERQF GKGSVMRMGD STVSRDIEAI STGSLGLDIA LGIGGLPKGR
IVEIYGPESS GKTTLTLQVI AECQKMGGTA AFIDAEHALD PSYAQKLGVK VDELLVSQPD
TGEQALEITD MLVRSAAVDV VIIDSVAALT PKAEIEGEMG DSHVGLQARL MSQALRKLTA
NIKRSNTLVI FINQIRMKIG VMFGSPETTT GGNALKFYAS VRLDIRRIGS IKKGEEILGS
ETRVKVVKNK VAPPFKMTEF DILYNEGISR ESEIINLGVQ LNLIEKSGAW YSYKQEKIGQ
GKENVRLYLK ENPQVAAELE QQIRTELLEK KLSVLASSSE DLFETIDD