位置:首页 > 蛋白库 > RECA_LACLM
RECA_LACLM
ID   RECA_LACLM              Reviewed;         387 AA.
AC   A2RI85;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=llmg_0374;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL96979.1; -; Genomic_DNA.
DR   RefSeq; WP_011675413.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; A2RI85; -.
DR   SMR; A2RI85; -.
DR   STRING; 416870.llmg_0374; -.
DR   PRIDE; A2RI85; -.
DR   EnsemblBacteria; CAL96979; CAL96979; llmg_0374.
DR   GeneID; 61108677; -.
DR   KEGG; llm:llmg_0374; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_9; -.
DR   OMA; DYGEQAL; -.
DR   PhylomeDB; A2RI85; -.
DR   BioCyc; LLAC416870:LLMG_RS01920-MON; -.
DR   Proteomes; UP000000364; 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   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..387
FT                   /note="Protein RecA"
FT                   /id="PRO_0000285246"
FT   REGION          348..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   387 AA;  41380 MW;  AF0B283F7FAAB335 CRC64;
     MATKKKTNFD DITKKYGAER DKALADALAL IEKDFGKGSL MRLGEAANQK VSVVSSGSLA
     LDIALGAGGY PKGRIVEIYG PESSGKTTVA LHAVAAVQKE GGIAAFIDAE NALDPEYAKA
     LGVNIDELLL SQPDYGEQGL QIAEKLITSG AVDLVVIDSV AALVPKAEID GEIGDSSVGL
     QARMMSQAMR KLAGHINKTK TTAIFINQLR EKVGVMFGSP ETTPGGRALK FYASVRLDVR
     GSTKIEEGSG DNKTQIGKIT KIKVVKNKVA PPFKVALVDI MFGEGISSTG ELLNIAVEEG
     IIKKSGAWFA YNDEKIGQGA EKAKNYLKEH QDVFDEIDHK VRAAHGLLDD SEVAETEEET
     TASKTKAKAK KEEKAVETEE IELELED
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024