TOPOM_MYCS2
ID TOPOM_MYCS2 Reviewed; 713 AA.
AC A0QPN1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Topoisomerase subunit TopoM {ECO:0000303|PubMed:16313624};
DE EC=5.6.2.2 {ECO:0000269|PubMed:16313624};
GN Name=topoM {ECO:0000303|PubMed:16313624};
GN OrderedLocusNames=MSMEG_0456, MSMEI_0443;
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).
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 (PubMed:16313624).
CC {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) (PubMed:16313624).
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 (PubMed:16313624).
CC {ECO:0000269|PubMed:16313624}.
CC -!- SUBUNIT: A complex of TopoN and TopoM, possibly a heterotetramer
CC (PubMed:16313624). {ECO:0000269|PubMed:16313624}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK76234.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36924.1; -; Genomic_DNA.
DR RefSeq; WP_003891777.1; NZ_SIJM01000025.1.
DR RefSeq; YP_884869.1; NC_008596.1.
DR AlphaFoldDB; A0QPN1; -.
DR SMR; A0QPN1; -.
DR STRING; 246196.MSMEI_0443; -.
DR EnsemblBacteria; ABK76234; ABK76234; MSMEG_0456.
DR EnsemblBacteria; AFP36924; AFP36924; MSMEI_0443.
DR GeneID; 66738639; -.
DR KEGG; msg:MSMEI_0443; -.
DR KEGG; msm:MSMEG_0456; -.
DR PATRIC; fig|246196.19.peg.451; -.
DR eggNOG; COG0188; Bacteria.
DR OMA; KLNPHGD; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR Pfam; PF03989; DNA_gyraseA_C; 2.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT CHAIN 1..713
FT /note="Topoisomerase subunit TopoM"
FT /id="PRO_0000434909"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 77225 MW; 46E1A2377B46C603 CRC64;
MTATLDVPEQ NPDLVLDQSA DDYWNHYQLT FALYSVSDRA IPSAYDGLKP GQRRLLYQMH
DSKLLPGNKP QKSSKVCSAV TGNLHPHGGA SMYGAAALMA ADFQRVKVID GQGAFPRIQG
DIPAADRYTE MRLSAPGAAL TAELNDHAVP MVPTFDGEWV EPTVLPAQWP VLLCNGAVGI
AEGWATKVPA HNPREVMAAC RALLKTPNMT DDRLCKLIPG PDWGSGASVV GTAGLREYIT
TGRGHFTVRG TISVEGKNCI ITELPPGVAS NTVQDRIRAL VESGEMSGVA DMSDLTDRRN
GLRIVVTAKR GHNAEQIRDQ LLALTPLEST FAASLVALDE NRVPRWWSVR DLIMAFLQLR
DSVVLHRSEY RLEKVTARRH LVAGLMKIHL DIDAAVAVIR GSETVDEARK GLQERFKIDA
EQADYVLSLQ LRRLTKLDVI ELQAEAEKLD AEFAELNDLV TNPESRRKVI DKELVETAKL
FKGPEYDRRT VLDFDATPVS RGDEDGSRER KVNTAWRLDD RGVFSDSHGE LLTSGLGWAV
WSDGRIKFTT GNGLPFKIRD IPVAPDITGL VRSGVLPEGY HLALVTRRGK ILRVDPASVN
PQGVAGNGVA GVKLAADGDE VIAALPVSCA NGEAILSIAE KSWKVTEVAD IPVKGRGGAG
VAFHPFVKGE DALLAASISK TGYVRGKRAV RPENRAKASI KGSGADVTPA PAE