RECA_AMYMU
ID RECA_AMYMU Reviewed; 348 AA.
AC Q9REV6; D8HUU2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=AMED_2343;
OS Amycolatopsis mediterranei (strain U-32).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=749927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gao J., Jiang W., Zhao G., Chiao J.;
RT "Amycolatopsis mediterranei recA, recX genes.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-32;
RX PubMed=20567260; DOI=10.1038/cr.2010.87;
RA Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., Zhang Z.,
RA Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., Ding X.,
RA Zhao G.P.;
RT "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT mediterranei U32 revealed its genetic characteristics in phylogeny and
RT metabolism.";
RL Cell Res. 20:1096-1108(2010).
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; AF208682; AAF19203.1; -; Genomic_DNA.
DR EMBL; CP002000; ADJ44140.1; -; Genomic_DNA.
DR RefSeq; WP_013224217.1; NC_014318.1.
DR RefSeq; YP_003764542.1; NC_014318.1.
DR AlphaFoldDB; Q9REV6; -.
DR SMR; Q9REV6; -.
DR STRING; 749927.AMED_2343; -.
DR EnsemblBacteria; ADJ44140; ADJ44140; AMED_2343.
DR KEGG; amd:AMED_2343; -.
DR PATRIC; fig|749927.5.peg.2417; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_1_2_11; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000000328; 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..348
FT /note="Protein RecA"
FT /id="PRO_0000122638"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 348 AA; 37084 MW; D58261A69290DEB4 CRC64;
MPAAPDKDKA LELALAQIDK QYGKGSVMRL GEEGRAPIAV IPTGAIALDV ALGIGGLPRG
RVIEVYGPES SGKTTVALHA VANAQRNGGI AAFIDAEHAL DPDYAKKLGV DTDALLVSQP
DTGEQALEIA DMLVRSGALD ILVIDSVAAL VPRAEIEGEM GDSHVGLQAR LMSQALRKMT
GAMNNSGTTA IFINQLREKI GVMFGSPETT TGGKALKFYA SVRLDVRRIE TLKDGGEAVG
NRTRVKVVKN KMAPPFKQAE FDILYGHGIS REGSLIDMGV DQAILRKSGA WYTYEGDQLG
QGKENARKFL RDNPDIANEI EKRIKEKLGI GAQLDAEAVE AVPAPVDF
