RECA_MYCTU
ID RECA_MYCTU Reviewed; 790 AA.
AC P9WHJ3; L0TAH5; O34519; P0A5U4; P26345;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
DE Contains:
DE RecName: Full=Endonuclease PI-MtuI;
DE EC=3.1.-.-;
DE AltName: Full=Mtu RecA intein;
GN Name=recA; OrderedLocusNames=Rv2737c; ORFNames=MTV002.02c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=1909321; DOI=10.1128/jb.173.18.5653-5662.1991;
RA Davis E.O., Sedgwick S.G., Colston M.J.;
RT "Novel structure of the recA locus of Mycobacterium tuberculosis implies
RT processing of the gene product.";
RL J. Bacteriol. 173:5653-5662(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canetti, and SO93;
RA Vansoolingen D., Hoogenboezem T., Dehaas P.E., Hermans P.W.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP PROTEIN SPLICING.
RX PubMed=1423588; DOI=10.1016/0092-8674(92)90349-h;
RA Davis E.O., Jenner P.J., Brooks P.C., Colston M.J., Sedgwick S.G.;
RT "Protein splicing in the maturation of M. tuberculosis recA protein: a
RT mechanism for tolerating a novel class of intervening sequence.";
RL Cell 71:201-210(1992).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8639660; DOI=10.1021/bi9517751;
RA Kumar R.A., Vaze M.B., Chandra N.R., Vijayan M., Muniyappa K.;
RT "Functional characterization of the precursor and spliced forms of RecA
RT protein of Mycobacterium tuberculosis.";
RL Biochemistry 35:1793-1802(1996).
RN [6]
RP REVIEW.
RA Colston M.J., Davis E.O.;
RL (In) Bloom B.R. (eds.);
RL Tuberculosis: pathogenesis, protection and control, pp.217-226, American
RL Society for Microbiology, Washington D.C. (1994).
RN [7]
RP INTERACTION WITH UVRD1 AND UVRA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20455546; DOI=10.1021/bi902021d;
RA Singh P., Patil K.N., Khanduja J.S., Kumar P.S., Williams A., Rossi F.,
RA Rizzi M., Davis E.O., Muniyappa K.;
RT "Mycobacterium tuberculosis UvrD1 and UvrA proteins suppress DNA strand
RT exchange promoted by cognate and noncognate RecA proteins.";
RL Biochemistry 49:4872-4883(2010).
RN [8]
RP PUPYLATION AT LYS-762, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [10]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=32634279; DOI=10.1111/mmi.14571;
RA Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT DNA-damage response and leads to cell death.";
RL Mol. Microbiol. 114:641-652(2020).
RN [11]
RP INDUCTION BY DNA DAMAGE AND BY DART.
RC STRAIN=H37Rv;
RX PubMed=34408320; DOI=10.1038/s41586-021-03825-4;
RA Schuller M., Butler R.E., Ariza A., Tromans-Coia C., Jankevicius G.,
RA Claridge T.D.W., Kendall S.L., Goh S., Stewart G.R., Ahel I.;
RT "Molecular basis for DarT ADP-ribosylation of a DNA base.";
RL Nature 596:597-602(2021).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=11121488; DOI=10.1093/nar/28.24.4964;
RA Datta S., Prabu M.M., Vaze M.B., Ganesh N., Chandra N.R., Muniyappa K.,
RA Vijayan M.;
RT "Crystal structures of Mycobacterium tuberculosis RecA and its complex with
RT ADP-AlF(4): implications for decreased ATPase activity and molecular
RT aggregation.";
RL Nucleic Acids Res. 28:4964-4973(2000).
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.
CC -!- FUNCTION: PI-MtuI is an endonuclease.
CC -!- SUBUNIT: Interacts with UvrD1 and UvrA (PubMed:20455546). Co-
CC immunoprecipitates with DarG in the presence and absence of darT
CC (PubMed:32634279). {ECO:0000269|PubMed:20455546,
CC ECO:0000269|PubMed:32634279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By DNA damage, and by ADP-ribosylation catalyzed by DarT (at
CC protein level). {ECO:0000269|PubMed:34408320}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
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DR EMBL; X58485; CAA41395.1; -; Genomic_DNA.
DR EMBL; AJ000012; CAA03857.1; -; Genomic_DNA.
DR EMBL; AJ000011; CAA03856.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45535.1; -; Genomic_DNA.
DR PIR; S18206; S18206.
DR RefSeq; NP_217253.1; NC_000962.3.
DR RefSeq; WP_003414006.1; NZ_NVQJ01000017.1.
DR PDB; 1G18; X-ray; 3.80 A; A=1-790.
DR PDB; 1G19; X-ray; 3.00 A; A=1-790.
DR PDB; 1MO3; X-ray; 3.10 A; A=1-790.
DR PDB; 1MO4; X-ray; 3.20 A; A=1-790.
DR PDB; 1MO5; X-ray; 3.25 A; A=1-790.
DR PDB; 1MO6; X-ray; 3.20 A; A=1-790.
DR PDB; 2IMZ; X-ray; 1.70 A; A/B=252-691.
DR PDB; 2IN0; X-ray; 1.60 A; A=252-691.
DR PDB; 2IN8; X-ray; 1.70 A; A=252-691.
DR PDB; 2IN9; X-ray; 1.80 A; A=252-691.
DR PDB; 2L8L; NMR; -; A=252-345, A=654-691.
DR PDB; 3IFJ; X-ray; 1.90 A; A/B=252-691.
DR PDB; 3IGD; X-ray; 2.40 A; A=252-691.
DR PDB; 4OQF; X-ray; 2.80 A; A=1-771.
DR PDB; 4PO1; X-ray; 3.40 A; A=1-790.
DR PDB; 4PO8; X-ray; 2.70 A; A=1-790.
DR PDB; 4PO9; X-ray; 2.75 A; A=1-790.
DR PDB; 4POA; X-ray; 2.95 A; A=1-790.
DR PDB; 4PPF; X-ray; 2.30 A; A=1-790.
DR PDB; 4PPG; X-ray; 3.00 A; A=1-790.
DR PDB; 4PPN; X-ray; 2.60 A; A=1-790.
DR PDB; 4PPQ; X-ray; 2.85 A; A=1-790.
DR PDB; 4PQF; X-ray; 2.80 A; A=1-790.
DR PDB; 4PQR; X-ray; 2.80 A; A=1-790.
DR PDB; 4PQY; X-ray; 2.95 A; A=1-790.
DR PDB; 4PR0; X-ray; 2.60 A; A=1-790.
DR PDB; 4PSA; X-ray; 2.65 A; A=1-790.
DR PDB; 4PSK; X-ray; 2.80 A; A=1-790.
DR PDB; 4PSV; X-ray; 2.60 A; A=1-790.
DR PDB; 4PTL; X-ray; 2.50 A; A=1-790.
DR PDB; 5I0A; X-ray; 1.50 A; A=252-696.
DR PDB; 5K08; X-ray; 1.40 A; A=252-694.
DR PDBsum; 1G18; -.
DR PDBsum; 1G19; -.
DR PDBsum; 1MO3; -.
DR PDBsum; 1MO4; -.
DR PDBsum; 1MO5; -.
DR PDBsum; 1MO6; -.
DR PDBsum; 2IMZ; -.
DR PDBsum; 2IN0; -.
DR PDBsum; 2IN8; -.
DR PDBsum; 2IN9; -.
DR PDBsum; 2L8L; -.
DR PDBsum; 3IFJ; -.
DR PDBsum; 3IGD; -.
DR PDBsum; 4OQF; -.
DR PDBsum; 4PO1; -.
DR PDBsum; 4PO8; -.
DR PDBsum; 4PO9; -.
DR PDBsum; 4POA; -.
DR PDBsum; 4PPF; -.
DR PDBsum; 4PPG; -.
DR PDBsum; 4PPN; -.
DR PDBsum; 4PPQ; -.
DR PDBsum; 4PQF; -.
DR PDBsum; 4PQR; -.
DR PDBsum; 4PQY; -.
DR PDBsum; 4PR0; -.
DR PDBsum; 4PSA; -.
DR PDBsum; 4PSK; -.
DR PDBsum; 4PSV; -.
DR PDBsum; 4PTL; -.
DR PDBsum; 5I0A; -.
DR PDBsum; 5K08; -.
DR AlphaFoldDB; P9WHJ3; -.
DR SMR; P9WHJ3; -.
DR STRING; 83332.Rv2737c; -.
DR BindingDB; P9WHJ3; -.
DR ChEMBL; CHEMBL1741171; -.
DR MEROPS; N10.009; -.
DR PaxDb; P9WHJ3; -.
DR GeneID; 888371; -.
DR KEGG; mtu:Rv2737c; -.
DR TubercuList; Rv2737c; -.
DR eggNOG; COG0468; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR OMA; MAPSMEY; -.
DR PhylomeDB; P9WHJ3; -.
DR PRO; PR:P9WHJ3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:MTBBASE.
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:0000150; F:DNA strand exchange activity; IDA:MTBBASE.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MTBBASE.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:MTBBASE.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IMP:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR GO; GO:0042148; P:strand invasion; IDA:MTBBASE.
DR GO; GO:0009650; P:UV protection; IMP:MTBBASE.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.10.28.10; -; 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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00379; INTEIN.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Endonuclease; Hydrolase;
KW Intron homing; Isopeptide bond; Nuclease; Nucleotide-binding;
KW Protein splicing; Reference proteome; SOS response; Ubl conjugation.
FT CHAIN 1..251
FT /note="Protein RecA, 1st part"
FT /id="PRO_0000030269"
FT CHAIN 252..691
FT /note="Endonuclease PI-MtuI"
FT /id="PRO_0000030270"
FT CHAIN 692..790
FT /note="Protein RecA, 2nd part"
FT /id="PRO_0000030271"
FT DOMAIN 366..508
FT /note="DOD-type homing endonuclease"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CROSSLNK 762
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT VARIANT 305
FT /note="R -> Q (in strain: Canetti and SO93)"
FT VARIANT 430
FT /note="A -> L (in strain: Canetti and SO93)"
FT VARIANT 434..435
FT /note="QQ -> RR (in strain: Canetti and SO93)"
FT VARIANT 438..439
FT /note="IY -> VH (in strain: Canetti and SO93)"
FT HELIX 5..22
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4OQF"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:4PPF"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 237..252
FT /evidence="ECO:0007829|PDB:4PPF"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5K08"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5K08"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2IN8"
FT STRAND 291..312
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5K08"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5K08"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5K08"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:2IN0"
SQ SEQUENCE 790 AA; 85389 MW; AD16340D2ED5E572 CRC64;
MTQTPDREKA LELAVAQIEK SYGKGSVMRL GDEARQPISV IPTGSIALDV ALGIGGLPRG
RVIEIYGPES SGKTTVALHA VANAQAAGGV AAFIDAEHAL DPDYAKKLGV DTDSLLVSQP
DTGEQALEIA DMLIRSGALD IVVIDSVAAL VPRAELEGEM GDSHVGLQAR LMSQALRKMT
GALNNSGTTA IFINQLRDKI GVMFGSPETT TGGKALKFYA SVRMDVRRVE TLKDGTNAVG
NRTRVKVVKN KCLAEGTRIF DPVTGTTHRI EDVVDGRKPI HVVAAAKDGT LHARPVVSWF
DQGTRDVIGL RIAGGAIVWA TPDHKVLTEY GWRAAGELRK GDRVAQPRRF DGFGDSAPIP
ADHARLLGYL IGDGRDGWVG GKTPINFINV QRALIDDVTR IAATLGCAAH PQGRISLAIA
HRPGERNGVA DLCQQAGIYG KLAWEKTIPN WFFEPDIAAD IVGNLLFGLF ESDGWVSREQ
TGALRVGYTT TSEQLAHQIH WLLLRFGVGS TVRDYDPTQK RPSIVNGRRI QSKRQVFEVR
ISGMDNVTAF AESVPMWGPR GAALIQAIPE ATQGRRRGSQ ATYLAAEMTD AVLNYLDERG
VTAQEAAAMI GVASGDPRGG MKQVLGASRL RRDRVQALAD ALDDKFLHDM LAEELRYSVI
REVLPTRRAR TFDLEVEELH TLVAEGVVVH NCSPPFKQAE FDILYGKGIS REGSLIDMGV
DQGLIRKSGA WFTYEGEQLG QGKENARNFL VENADVADEI EKKIKEKLGI GAVVTDDPSN
DGVLPAPVDF
