RECA_MYCS2
ID RECA_MYCS2 Reviewed; 349 AA.
AC Q59560; A0QVW9; I7G989;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
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};
GN OrderedLocusNames=MSMEG_2723, MSMEI_2656;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9822818; DOI=10.1046/j.1365-2958.1998.01083.x;
RA Papavinasasundaram K.G., Colston M.J., Davis E.O.;
RT "Construction and complementation of a recA deletion mutant of
RT Mycobacterium smegmatis reveals that the intein in Mycobacterium
RT tuberculosis recA does not affect RecA function.";
RL Mol. Microbiol. 30:525-534(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17360246; DOI=10.1016/j.dnarep.2007.02.009;
RA Pitcher R.S., Green A.J., Brzostek A., Korycka-Machala M., Dziadek J.,
RA Doherty A.J.;
RT "NHEJ protects mycobacteria in stationary phase against the harmful effects
RT of desiccation.";
RL DNA Repair 6:1271-1276(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17496093; DOI=10.1128/jb.00332-07;
RA Stephanou N.C., Gao F., Bongiorno P., Ehrt S., Schnappinger D., Shuman S.,
RA Glickman M.S.;
RT "Mycobacterial nonhomologous end joining mediates mutagenic repair of
RT chromosomal double-strand DNA breaks.";
RL J. Bacteriol. 189:5237-5246(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21219454; DOI=10.1111/j.1365-2958.2010.07463.x;
RA Gupta R., Barkan D., Redelman-Sidi G., Shuman S., Glickman M.S.;
RT "Mycobacteria exploit three genetically distinct DNA double-strand break
RT repair pathways.";
RL Mol. Microbiol. 79:316-330(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) WITH AND WITHOUT ATP.
RX PubMed=12837805; DOI=10.1128/jb.185.14.4280-4284.2003;
RA Datta S., Krishna R., Ganesh N., Chandra N.R., Muniyappa K., Vijayan M.;
RT "Crystal structures of Mycobacterium smegmatis RecA and its nucleotide
RT complexes.";
RL J. Bacteriol. 185:4280-4284(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) WITH AND WITHOUT ATP.
RX PubMed=17306300; DOI=10.1016/j.jmb.2007.01.058;
RA Krishna R., Prabu J.R., Manjunath G.P., Datta S., Chandra N.R.,
RA Muniyappa K., Vijayan M.;
RT "Snapshots of RecA protein involving movement of the C-domain and different
RT conformations of the DNA-binding loops: crystallographic and comparative
RT analysis of 11 structures of Mycobacterium smegmatis RecA.";
RL J. Mol. Biol. 367:1130-1144(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) WITH AND WITHOUT ATP AND PHOSPHATE,
RP AND MUTAGENESIS OF GLN-196.
RX PubMed=19020353; DOI=10.1107/s0907444908028448;
RA Prabu J.R., Manjunath G.P., Chandra N.R., Muniyappa K., Vijayan M.;
RT "Functionally important movements in RecA molecules and filaments: studies
RT involving mutation and environmental changes.";
RL Acta Crystallogr. D 64:1146-1157(2008).
CC -!- FUNCTION: Required for homologous recombination (HR) and the bypass of
CC mutagenic DNA lesions (double strand breaks, DSB) by the SOS response.
CC Can catalyze the hydrolysis of ATP in the presence of single-stranded
CC DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and
CC the ATP-dependent hybridization of homologous single-stranded DNAs.
CC Numerous X-ray crystals have been resolved under different conditions
CC which indicate the flexibility of the protein, essential to its
CC function. Gln-196 contributes to this plasticity by acting as a switch
CC residue, which transmits the effect of nucleotide binding to the DNA-
CC binding region. {ECO:0000269|PubMed:17360246,
CC ECO:0000269|PubMed:17496093, ECO:0000269|PubMed:21219454}.
CC -!- SUBUNIT: Polymerizes non-specifically on ssDNA to form filaments.
CC Interacts with and activates LexA leading to autocatalytic cleavage of
CC LexA, which derepresses the SOS regulon and activates DNA repair (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- DISRUPTION PHENOTYPE: Not essential in the absence of DNA damage, its
CC deletion renders cells much more sensitive to DNA damaging agents such
CC as UV light, ionizing radiation, alkylating agents and DNA gyrase
CC inhibitors and desiccation-induced DSBs. 5-fold decrease in survival,
CC loss of HR, no change in NHEJ (non-homologous end-joining) or single-
CC strand annealing DSB repair. {ECO:0000269|PubMed:17360246,
CC ECO:0000269|PubMed:17496093, ECO:0000269|PubMed:21219454}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; X99208; CAA67597.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK74334.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39124.1; -; Genomic_DNA.
DR RefSeq; WP_003894107.1; NZ_SIJM01000032.1.
DR RefSeq; YP_887057.1; NC_008596.1.
DR PDB; 1UBC; X-ray; 3.80 A; A=1-349.
DR PDB; 1UBE; X-ray; 3.30 A; A=1-349.
DR PDB; 1UBF; X-ray; 3.50 A; A=1-349.
DR PDB; 1UBG; X-ray; 3.50 A; A=1-349.
DR PDB; 2G88; X-ray; 3.20 A; A=1-349.
DR PDB; 2ODN; X-ray; 3.10 A; A=1-349.
DR PDB; 2ODW; X-ray; 3.30 A; A=1-349.
DR PDB; 2OE2; X-ray; 3.45 A; A=1-349.
DR PDB; 2OEP; X-ray; 3.10 A; A=1-349.
DR PDB; 2OES; X-ray; 3.50 A; A=1-349.
DR PDB; 2OFO; X-ray; 3.16 A; A=1-349.
DR PDB; 2ZR0; X-ray; 3.00 A; A=1-349.
DR PDB; 2ZR7; X-ray; 3.60 A; A=1-349.
DR PDB; 2ZR9; X-ray; 2.50 A; A=1-349.
DR PDB; 2ZRA; X-ray; 3.10 A; A=1-349.
DR PDB; 2ZRB; X-ray; 3.25 A; A=1-349.
DR PDB; 2ZRC; X-ray; 3.10 A; A=1-349.
DR PDB; 2ZRD; X-ray; 3.10 A; A=1-349.
DR PDB; 2ZRE; X-ray; 2.90 A; A=1-349.
DR PDB; 2ZRF; X-ray; 3.00 A; A=1-349.
DR PDB; 2ZRG; X-ray; 3.50 A; A=1-349.
DR PDB; 2ZRH; X-ray; 3.20 A; A=1-349.
DR PDB; 2ZRI; X-ray; 3.30 A; A=1-349.
DR PDB; 2ZRJ; X-ray; 2.60 A; A=1-349.
DR PDB; 2ZRK; X-ray; 3.20 A; A=1-349.
DR PDB; 2ZRL; X-ray; 3.70 A; A=1-349.
DR PDB; 2ZRM; X-ray; 2.80 A; A=1-349.
DR PDB; 2ZRN; X-ray; 3.30 A; A=1-349.
DR PDB; 2ZRO; X-ray; 2.90 A; A=1-349.
DR PDB; 2ZRP; X-ray; 3.30 A; A=1-349.
DR PDBsum; 1UBC; -.
DR PDBsum; 1UBE; -.
DR PDBsum; 1UBF; -.
DR PDBsum; 1UBG; -.
DR PDBsum; 2G88; -.
DR PDBsum; 2ODN; -.
DR PDBsum; 2ODW; -.
DR PDBsum; 2OE2; -.
DR PDBsum; 2OEP; -.
DR PDBsum; 2OES; -.
DR PDBsum; 2OFO; -.
DR PDBsum; 2ZR0; -.
DR PDBsum; 2ZR7; -.
DR PDBsum; 2ZR9; -.
DR PDBsum; 2ZRA; -.
DR PDBsum; 2ZRB; -.
DR PDBsum; 2ZRC; -.
DR PDBsum; 2ZRD; -.
DR PDBsum; 2ZRE; -.
DR PDBsum; 2ZRF; -.
DR PDBsum; 2ZRG; -.
DR PDBsum; 2ZRH; -.
DR PDBsum; 2ZRI; -.
DR PDBsum; 2ZRJ; -.
DR PDBsum; 2ZRK; -.
DR PDBsum; 2ZRL; -.
DR PDBsum; 2ZRM; -.
DR PDBsum; 2ZRN; -.
DR PDBsum; 2ZRO; -.
DR PDBsum; 2ZRP; -.
DR AlphaFoldDB; Q59560; -.
DR SMR; Q59560; -.
DR STRING; 246196.MSMEI_2656; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR DrugBank; DB03222; dATP.
DR PRIDE; Q59560; -.
DR EnsemblBacteria; ABK74334; ABK74334; MSMEG_2723.
DR EnsemblBacteria; AFP39124; AFP39124; MSMEI_2656.
DR GeneID; 66734128; -.
DR KEGG; msg:MSMEI_2656; -.
DR KEGG; msm:MSMEG_2723; -.
DR PATRIC; fig|246196.19.peg.2690; -.
DR eggNOG; COG0468; Bacteria.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR EvolutionaryTrace; Q59560; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..349
FT /note="Protein RecA"
FT /id="PRO_0000122767"
FT BINDING 71..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12837805,
FT ECO:0000269|PubMed:19020353"
FT BINDING 71..75
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:19020353"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12837805,
FT ECO:0000269|PubMed:19020353"
FT BINDING 196
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:19020353"
FT MUTAGEN 196
FT /note="Q->A,E,N: Loss of residue movement, loss of switch
FT function in crystal structures."
FT /evidence="ECO:0000269|PubMed:19020353"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2ZRP"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1UBG"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:2ZR9"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2ZRM"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1UBG"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1UBG"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2ZRJ"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 222..233
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 241..254
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2ZRE"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2ZR9"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:2ZR9"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:2ZR9"
SQ SEQUENCE 349 AA; 37301 MW; D85D21F5BFC5A020 CRC64;
MAQQAPDREK ALELAMAQID KNFGKGSVMR LGEEVRQPIS VIPTGSISLD VALGIGGLPR
GRVIEIYGPE SSGKTTVALH AVANAQAAGG IAAFIDAEHA LDPEYAKKLG VDTDSLLVSQ
PDTGEQALEI ADMLVRSGAL DIIVIDSVAA LVPRAEIEGE MGDSHVGLQA RLMSQALRKM
TGALNNSGTT AIFINQLREK IGVMFGSPET TTGGKALKFY ASVRLDVRRI ETLKDGTDAV
GNRTRVKVVK NKVSPPFKQA EFDILYGQGI SREGSLIDMG VEHGFIRKSG SWFTYEGEQL
GQGKENARKF LLENTDVANE IEKKIKEKLG IGAVVTAEAD DVLPAPVDF
