END4_MYCTU
ID END4_MYCTU Reviewed; 252 AA.
AC P9WQ13; L0T772; O86366; P63535;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152};
DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152};
DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
GN Name=end; Synonyms=nfo; OrderedLocusNames=Rv0670; ORFNames=MTCI376.04c;
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 [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 [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19027363; DOI=10.1016/j.tube.2008.09.002;
RA Santangelo Mde L., Blanco F., Campos E., Soria M., Bianco M.V., Klepp L.,
RA Alito A., Zabal O., Cataldi A., Bigi F.;
RT "Mce2R from Mycobacterium tuberculosis represses the expression of the mce2
RT operon.";
RL Tuberculosis 89:22-28(2009).
RN [3]
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).
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152};
CC -!- INDUCTION: Repressed by transcription regulator Mce2R.
CC {ECO:0000269|PubMed:19027363}.
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00152}.
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DR EMBL; AL123456; CCP43413.1; -; Genomic_DNA.
DR PIR; G70825; G70825.
DR RefSeq; NP_215184.1; NC_000962.3.
DR RefSeq; WP_003403419.1; NZ_NVQJ01000007.1.
DR PDB; 5ZHZ; X-ray; 1.18 A; A=1-252.
DR PDBsum; 5ZHZ; -.
DR AlphaFoldDB; P9WQ13; -.
DR SMR; P9WQ13; -.
DR STRING; 83332.Rv0670; -.
DR PaxDb; P9WQ13; -.
DR DNASU; 888190; -.
DR GeneID; 888190; -.
DR KEGG; mtu:Rv0670; -.
DR TubercuList; Rv0670; -.
DR eggNOG; COG0648; Bacteria.
DR OMA; HPGSHLK; -.
DR PhylomeDB; P9WQ13; -.
DR BRENDA; 3.1.21.2; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR CDD; cd00019; AP2Ec; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome; Zinc.
FT CHAIN 1..252
FT /note="Probable endonuclease 4"
FT /id="PRO_0000190860"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5ZHZ"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:5ZHZ"
SQ SEQUENCE 252 AA; 26845 MW; 170F550442C45A15 CRC64;
MLIGSHVSPT DPLAAAEAEG ADVVQIFLGN PQSWKAPKPR DDAAALKAAT LPIYVHAPYL
INLASANNRV RIPSRKILQE TCAAAADIGA AAVIVHGGHV ADDNDIDKGF QRWRKALDRL
ETEVPVYLEN TAGGDHAMAR RFDTIARLWD VIGDTGIGFC LDTCHTWAAG EALTDAVDRI
KAITGRIDLV HCNDSRDEAG SGRDRHANLG SGQIDPDLLV AAVKAAGAPV ICETADQGRK
DDIAFLRERT GS
