ID   TOPON_MYCS2             Reviewed;         698 AA.
AC   A0QPN2; I7F5Q2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Topoisomerase subunit TopoN {ECO:0000303|PubMed:16313624};
DE            EC=5.6.2.2 {ECO:0000269|PubMed:16313624};
DE   AltName: Full=DNA gyrase subunit B-like protein MSMEG_0457/MSMEI_0444;
GN   Name=topoN {ECO:0000303|PubMed:16313624};
GN   OrderedLocusNames=MSMEG_0457, MSMEI_0444;
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 [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   [2]
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   [3]
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   [4]
RP   FUNCTION, REACTION MECHANISM, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, AND SUBUNIT.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=16313624; DOI=10.1111/j.1365-2958.2005.04908.x;
RA   Jain P., Nagaraja V.;
RT   "An atypical type II topoisomerase from Mycobacterium smegmatis with
RT   positive supercoiling activity.";
RL   Mol. Microbiol. 58:1392-1405(2005).
RN   [5]
RP   PUPYLATION AT LYS-429, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- FUNCTION: Catalyzes the relaxation of negatively supercoiled DNA in the
CC       presence of ATP or dATP but not other nucleotides. Individual subunits
CC       have no activity. Not able to negatively supercoil DNA, it can however
CC       introduce positive supercoils in DNA. Relaxes positive supercoils in an
CC       ATP-dependent manner. Catenates and decatenates DNA. Generates dsDNA
CC       breaks in the presence of the quinolone antibiotic ciprofloxacin,
CC       showing it is a topoisomerase. {ECO:0000269|PubMed:16313624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000269|PubMed:16313624};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16313624};
CC       Note=Maximal DNA relaxation at 5.0 mM MgCl(2).
CC       {ECO:0000269|PubMed:16313624};
CC   -!- ACTIVITY REGULATION: Inhibited by quinolone antibiotic ciprofloxacin
CC       and coumarin antibiotic novobiocin, but at much higher concentrations
CC       than is usual for DNA gyrase/topoisomerase.
CC       {ECO:0000269|PubMed:16313624}.
CC   -!- SUBUNIT: A complex of TopoN and TopoM, possibly a heterotetramer.
CC       {ECO:0000269|PubMed:16313624}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK70935.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:16313624};
CC       Sequence=AFP36925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:16313624};
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DR   EMBL; CP000480; ABK70935.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP36925.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_884870.1; NC_008596.1.
DR   AlphaFoldDB; A0QPN2; -.
DR   SMR; A0QPN2; -.
DR   STRING; 246196.MSMEI_0444; -.
DR   EnsemblBacteria; ABK70935; ABK70935; MSMEG_0457.
DR   EnsemblBacteria; AFP36925; AFP36925; MSMEI_0444.
DR   KEGG; msg:MSMEI_0444; -.
DR   KEGG; msm:MSMEG_0457; -.
DR   PATRIC; fig|246196.19.peg.452; -.
DR   eggNOG; COG0187; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Isomerase; Isopeptide bond; Nucleotide-binding;
KW   Reference proteome; Topoisomerase; Ubl conjugation.
FT   CHAIN           1..698
FT                   /note="Topoisomerase subunit TopoN"
FT                   /id="PRO_0000396100"
FT   DOMAIN          479..593
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   REGION          443..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        429
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   698 AA;  74445 MW;  BD2A231A7D4CB1D9 CRC64;
     MSDPASTIPP AHHPTFWRER AVSYTAADIT ELDDVQHTRL RPAVNLGLDV LNTALREIVD
     NAIEEVADPG HGGSTVTITL HADGSVSVAD DGRGLPVDTD PTTGKNGIVK TLGTARAGGK
     FSAHKDATST GAGLNGIGAA AAVFISARTD VTVRRDGKTF LQSFGRGYPG VFEGKEFDPE
     APFTRNDTQK LRGVSNRKPD LHGTEVRILF DPAIAPDSTL DIGEVLLRAH AAARMSPGVH
     LVVVDEGWPG EEVPPAVLEP FSGPWGTDTL LDLMCTAAGT PLPEVRAVVE GRGEYTTGRG
     PTPFRWSLTA GPAEPATVAA FCNTVRTPGG GSHLTAAIKG LSEALAERAS RMRDLGLAKN
     EEGPEPQDFA AVTALAVDTR APDVAWDSQA KTAVSSRSLN LAMAPDVARS VTIWAANPAN
     ADTVTLWSKL ALESARARRS AEGAKARARA ASKAKGLGTN LSLPPKLLPS RESGRGSGAE
     LFLCEGDSAL GTIKAARDAT FQAAFPLKGK PPNVYGFPLN KARAKDEFDA IERILGCGVR
     DHCDPELCRY DRILFASDAD PDGGNINSSL ISMFLDFYRP LVEAGMVYVT MPPLFVVKAG
     DERIYCQDES ERDAAVAQLK ASSNRRVEVQ RNKGLGEMDA DDFWNTVLDP QRRTVIRVRP
     DESEKKLHHT LFGGPPEGRR TWMADVAARV DTSALDLT