GYRA_MYCS2
ID GYRA_MYCS2 Reviewed; 842 AA.
AC P48354; A0QNE1; I7FC85;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN OrderedLocusNames=MSMEG_0006, MSMEI_0008;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=8878580; DOI=10.1128/aac.40.9.2054;
RA Revel-Viravau V., Truong Q.C., Moreau N., Jarlier V., Sougakoff W.;
RT "Sequence analysis, purification, and study of inhibition by 4-quinolones
RT of the DNA gyrase from Mycobacterium smegmatis.";
RL Antimicrob. Agents Chemother. 40:2054-2061(1996).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner
CC (PubMed:8878580) to modulate DNA topology and maintain chromosomes in
CC an underwound state. Negative supercoiling favors strand separation,
CC and DNA replication, transcription, recombination and repair, all of
CC which involve strand separation. Also able to catalyze the
CC interconversion of other topological isomers of dsDNA rings, including
CC catenanes and knotted rings. Type II topoisomerases break and join 2
CC DNA strands simultaneously in an ATP-dependent manner.
CC {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:8878580}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01897};
CC -!- ACTIVITY REGULATION: Inhibited by 4-quinoline drugs (nalidixic acid,
CC ciprofloxacin, ofloxacin), although it is much less sensitive than the
CC corresponding enzyme from E.coli (PubMed:8878580).
CC {ECO:0000269|PubMed:8878580}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:8878580). In the heterotetramer, GyrA contains the active site
CC tyrosine that forms a transient covalent intermediate with DNA, while
CC GyrB binds cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-
CC Rule:MF_01897, ECO:0000269|PubMed:8878580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; X94224; CAA63918.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK69994.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36493.1; -; Genomic_DNA.
DR RefSeq; WP_003891334.1; NZ_SIJM01000001.1.
DR RefSeq; YP_884429.1; NC_008596.1.
DR AlphaFoldDB; P48354; -.
DR SMR; P48354; -.
DR STRING; 246196.MSMEI_0008; -.
DR PRIDE; P48354; -.
DR EnsemblBacteria; ABK69994; ABK69994; MSMEG_0006.
DR EnsemblBacteria; AFP36493; AFP36493; MSMEI_0008.
DR GeneID; 66738198; -.
DR KEGG; msg:MSMEI_0008; -.
DR KEGG; msm:MSMEG_0006; -.
DR PATRIC; fig|246196.19.peg.6; -.
DR eggNOG; COG0188; Bacteria.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
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; 6.
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 Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..842
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145242"
FT REGION 822..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 538..544
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 826..842
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 842 AA; 93183 MW; 50AE5DBE80ED45DD CRC64;
MTDTTLPPEG EAHDRIEPVD IQQEMQRSYI DYAMSVIVGR ALPEVRDGLK PVHRRVLYAM
YDSGFRPDRS HAKSARSVAE TMGNYHPHGD ASIYDTLVRM AQPWSLRYPL VDGQGNFGSP
GNDPPAAMRY TEARLTPLAM EMLREIDEET VDFIPNYDGR VQEPTVLPSR FPNLLANGSG
GIAVGMATNI PPHNLGELAE AVYWCLENYE ADEEATCEAV MERVKGPDFP TSGLIVGTQG
IEDTYKTGRG SIKMRGVVEI EEDSRGRTSI VITELPYQVN HDNFITSIAE QVRDGKLAGI
SNIEDQSSDR VGLRIVVELK RDAVAKVVLN NLYKHTQLQT SFGANMLSIV DGVPRTLRLD
QLIRLYVDHQ LDVIVRRTRY RLRKANERAH ILRGLVKALD ALDEVIALIR ASQTVDIARA
GLIELLDIDD IQAQAILDMQ LRRLAALERQ KIVDDLAKIE AEIADLEDIL AKPERQRGIV
RDELKEIVDK HGDARRTRIV PADGEVSDED LIAREDVVVT ITETGYAKRT KTDLYRSQKR
GGKGVQGAGL KQDDMVNHFF VCSTHDWILF FTTQGRVYRA KAYELPEASR TARGQHVANL
LAFQPEERIA QVIQIKSYED APYLVLATRN GLVKKSKLSD FDSNRSGGIV AINLREGDEL
VGAVLCSAED DLLLVSANGQ SIRFSATDEA LRPMGRATSG VQGMRFNEDD RLLSLNVVRP
DTYLLVATSG GYAKRTSIDE YSVQGRGGKG ILTIQYDRKR GSLVGALIVD DDTELYAITS
TGGVIRTAAR QVRKAGRQTK GVRLMNLAEG DTLIAIARNA DEDEAAESIS ESDADTAESP
EA
