RECA_LEPIN
ID RECA_LEPIN Reviewed; 366 AA.
AC P52277;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=LA_2179;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Kenniwicki / Serogroup Pomona / Serovar pomona;
RA Yelton D.B., Salvitti J.A.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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}.
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DR EMBL; U29169; AAA98505.1; -; Genomic_DNA.
DR EMBL; AE010300; AAN49378.1; -; Genomic_DNA.
DR RefSeq; NP_712360.1; NC_004342.2.
DR RefSeq; WP_000504720.1; NC_004342.2.
DR AlphaFoldDB; P52277; -.
DR SMR; P52277; -.
DR STRING; 189518.LA_2179; -.
DR EnsemblBacteria; AAN49378; AAN49378; LA_2179.
DR GeneID; 61141643; -.
DR KEGG; lil:LA_2179; -.
DR PATRIC; fig|189518.3.peg.2171; -.
DR HOGENOM; CLU_040469_3_2_12; -.
DR InParanoid; P52277; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000001408; Chromosome I.
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; 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; 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; Reference proteome; SOS response.
FT CHAIN 1..366
FT /note="Protein RecA"
FT /id="PRO_0000122744"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 110
FT /note="A -> G (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..260
FT /note="IKEKEESVGNRVRVK -> TTEKDRICRNRDESN (in Ref. 1;
FT AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..267
FT /note="CA -> SCP (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="Q -> P (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="N -> NH (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> AS (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..331
FT /note="NPEIA -> KTLKLT (in Ref. 1; AAA98505)"
FT /evidence="ECO:0000305"
FT CONFLICT 345..366
FT /note="PLLVQENNKKSRKEEKLEQAAG -> TFVSSGK (in Ref. 1;
FT AAA98505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 39687 MW; 9F090E631CDF6E79 CRC64;
MGESIMKKAK EDAPSVDDSK KLAIEQAMSQ IEKQFGKGSI MKLGSDSAKQ TVQVIPSGSL
DLDIALGIGG YPIGRIVEIY GPESSGKTTL TLSAIAEAQK RGGVAAFIDA EHALDPSYAK
KLGVNIDELL VSQPDNGEEA LEICESLVRS NAIDLIVIDS VAALVPKAEI EGDMGDSHMG
LQARLMSQAL RKLTGTIAKS KTVVIFINQI RMKIGVMFGS PETTTGGNAL KFYCSVRLDI
RKIETIKEKE ESVGNRVRVK VVKNKCAPPF KQAEFDIIFN AGISREGSLV DLGVKHDIIH
KAGAWYSYNT EKIGQGKEAA KEYLKNNPEI ALTIENMVRD LNSLPLLVQE NNKKSRKEEK
LEQAAG
