DNAB_MYCTU
ID DNAB_MYCTU Reviewed; 874 AA.
AC P9WMR3; L0T2G0; P71715;
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=Replicative DNA helicase;
DE EC=3.6.4.12;
DE Contains:
DE RecName: Full=Endonuclease PI-MtuHIP;
DE EC=3.1.-.-;
DE AltName: Full=Mtu dnaB intein;
GN Name=dnaB; OrderedLocusNames=Rv0058; ORFNames=MTCY21D4.21;
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 IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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 [4]
RP OPERON STRUCTURE.
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).
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity. {ECO:0000250}.
CC -!- FUNCTION: The intein is an endonuclease. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Co-immunoprecipitates with DarG in the presence and absence of
CC darT. {ECO:0000269|PubMed:32634279}.
CC -!- INTERACTION:
CC P9WMR3; P9WGD5: ssb; NbExp=3; IntAct=EBI-9081402, EBI-9081374;
CC -!- INDUCTION: Part of the dnaB-darT-darG operon.
CC {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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42780.1; -; Genomic_DNA.
DR PIR; B70914; B70914.
DR RefSeq; NP_214572.1; NC_000962.3.
DR RefSeq; WP_003916208.1; NZ_NVQJ01000005.1.
DR PDB; 2R5U; X-ray; 1.90 A; A/B/C/D/E/F=1-197.
DR PDBsum; 2R5U; -.
DR AlphaFoldDB; P9WMR3; -.
DR SMR; P9WMR3; -.
DR IntAct; P9WMR3; 1.
DR MINT; P9WMR3; -.
DR STRING; 83332.Rv0058; -.
DR ChEMBL; CHEMBL1741192; -.
DR PaxDb; P9WMR3; -.
DR DNASU; 887009; -.
DR GeneID; 887009; -.
DR KEGG; mtu:Rv0058; -.
DR TubercuList; Rv0058; -.
DR eggNOG; COG0305; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR OMA; RSHEKFV; -.
DR PhylomeDB; P9WMR3; -.
DR PRO; PR:P9WMR3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:MTBBASE.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007692; DNA_helicase_DnaB.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
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 Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51199; SF4_HELICASE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autocatalytic cleavage; DNA replication;
KW DNA-binding; Endonuclease; Helicase; Hydrolase; Intron homing; Nuclease;
KW Nucleotide-binding; Primosome; Protein splicing; Reference proteome;
KW Repeat.
FT CHAIN 1..399
FT /note="Replicative DNA helicase, 1st part"
FT /id="PRO_0000013282"
FT CHAIN 400..815
FT /note="Endonuclease PI-MtuHIP"
FT /id="PRO_0000013283"
FT CHAIN 816..874
FT /note="Replicative DNA helicase, 2nd part"
FT /id="PRO_0000013284"
FT DOMAIN 195..462
FT /note="SF4 helicase; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT DOMAIN 582..660
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 612..874
FT /note="SF4 helicase; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 116..145
FT /evidence="ECO:0007829|PDB:2R5U"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2R5U"
SQ SEQUENCE 874 AA; 96917 MW; 894155A86DCB9D70 CRC64;
MAVVDDLAPG MDSSPPSEDY GRQPPQDLAA EQSVLGGMLL SKDAIADVLE RLRPGDFYRP
AHQNVYDAIL DLYGRGEPAD AVTVAAELDR RGLLRRIGGA PYLHTLISTV PTAANAGYYA
SIVAEKALLR RLVEAGTRVV QYGYAGAEGA DVAEVVDRAQ AEIYDVADRR LSEDFVALED
LLQPTMDEID AIASSGGLAR GVATGFTELD EVTNGLHPGQ MVIVAARPGV GKSTLGLDFM
RSCSIRHRMA SVIFSLEMSK SEIVMRLLSA EAKIKLSDMR SGRMSDDDWT RLARRMSEIS
EAPLFIDDSP NLTMMEIRAK ARRLRQKANL KLIVVDYLQL MTSGKKYESR QVEVSEFSRH
LKLLAKELEV PVVAISQLNR GPEQRTDKKP MLADLRESGC LTASTRILRA DTGAEVAFGE
LMRSGERPMV WSLDERLRMV ARPMINVFPS GRKEVFRLRL ASGREVEATG SHPFMKFEGW
TPLAQLKVGD RIAAPRRVPE PIDTQRMPES ELISLARMIG DGSCLKNQPI RYEPVDEANL
AAVTVSAAHS DRAAIRDDYL AARVPSLRPA RQRLPRGRCT PIAAWLAGLG LFTKRSHEKC
VPEAVFRAPN DQVALFLRHL WSAGGSVRWD PTNGQGRVYY GSTSRRLIDD VAQLLLRVGI
FSWITHAPKL GGHDSWRLHI HGAKDQVRFL RHVGVHGAEA VAAQEMLRQL KGPVRNPNLD
SAPKKVWAQV RNRLSAKQMM DIQLHEPTMW KHSPSRSRPH RAEARIEDRA IHELARGDAY
WDTVVEITSI GDQHVFDGTV SGTHNFVANG ISLHNSLEQD ADVVILLHRP DAFDRDDPRG
GEADFILAKH RNGPTKTVTV AHQLHLSRFA NMAR
