GYRA_MYCBP
ID GYRA_MYCBP Reviewed; 838 AA.
AC A0A0G2Q9F8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=gyrA1 {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=BCG_0006;
GN and
GN Name=gyrA2 {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=BCG_0036;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP POSSIBLE ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF ALA-90 AND ASP-94.
RC STRAIN=BCG / Pasteur;
RX PubMed=8031045; DOI=10.1128/aac.38.4.773;
RA Takiff H.E., Salazar L., Guerrero C., Philipp W., Huang W.M.,
RA Kreiswirth B., Cole S.T., Jacobs W.R. Jr., Telenti A.;
RT "Cloning and nucleotide sequence of Mycobacterium tuberculosis gyrA and
RT gyrB genes and detection of quinolone resistance mutations.";
RL Antimicrob. Agents Chemother. 38:773-780(1994).
RN [3]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=BCG / ATCC 27289 / DSM 43990;
RX PubMed=7503546; DOI=10.1006/abbi.1995.9919;
RA Wu L.C., Shahied S.I.;
RT "Mycobacterial DNA gyrase: enzyme purification and characterization of
RT supercoiling activity.";
RL Arch. Biochem. Biophys. 324:123-129(1995).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Also catalyzes the interconversion of other topological isomers of
CC double-stranded DNA rings, including catenanes and knotted rings.
CC Relaxes negatively supercoiled DNA in an ATP-independent manner. A
CC linear reaction intermediate can be trapped in the presence of the
CC antibiotic ciprofloxacin (PubMed:7503546). Negative supercoiling favors
CC strand separation, and DNA replication, transcription, recombination
CC and repair, all of which involve strand separation. Type II
CC topoisomerases break and join 2 DNA strands simultaneously in an ATP-
CC dependent manner. {ECO:0000269|PubMed:7503546}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7503546};
CC Note=Reaction requires Mg(2+). {ECO:0000269|PubMed:7503546};
CC -!- ACTIVITY REGULATION: DNA supercoiling is inhibited by EDTA, novobiocin,
CC coumermycin and ciprofloxacin (PubMed:7503546).
CC {ECO:0000269|PubMed:7503546}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:7503546). 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:7503546}.
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; AM408590; CAL69990.1; -; Genomic_DNA.
DR EMBL; AM408590; CAL70020.1; -; Genomic_DNA.
DR RefSeq; WP_003400286.1; NC_008769.1.
DR AlphaFoldDB; A0A0G2Q9F8; -.
DR SMR; A0A0G2Q9F8; -.
DR GeneID; 45423963; -.
DR KEGG; mbb:BCG_0006; -.
DR KEGG; mbb:BCG_0036; -.
DR HOGENOM; CLU_002977_6_1_11; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000001472; 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; Topoisomerase.
FT CHAIN 1..838
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000435478"
FT MOTIF 537..543
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 129
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT MUTAGEN 90
FT /note="A->V: Probably resistant to ciprofloxacin."
FT /evidence="ECO:0000269|PubMed:8031045"
FT MUTAGEN 94
FT /note="D->N: Probably resistant to ciprofloxacin."
FT /evidence="ECO:0000269|PubMed:8031045"
SQ SEQUENCE 838 AA; 92345 MW; 7EC969F3410373B9 CRC64;
MTDTTLPPDD SLDRIEPVDI QQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF
DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDTLVRMA QPWSLRYPLV DGQGNFGSPG
NDPPAAMRYT EARLTPLAME MLREIDEETV DFIPNYDGRV QEPTVLPSRF PNLLANGSGG
IAVGMATNIP PHNLRELADA VFWALENHDA DEEETLAAVM GRVKGPDFPT AGLIVGSQGT
ADAYKTGRGS IRMRGVVEVE EDSRGRTSLV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS
NIEDQSSDRV GLRIVIEIKR DAVAKVVINN LYKHTQLQTS FGANMLAIVD GVPRTLRLDQ
LIRYYVDHQL DVIVRRTTYR LRKANERAHI LRGLVKALDA LDEVIALIRA SETVDIARAG
LIELLDIDEI QAQAILDMQL RRLAALERQR IIDDLAKIEA EIADLEDILA KPERQRGIVR
DELAEIVDRH GDDRRTRIIA ADGDVSDEDL IAREDVVVTI TETGYAKRTK TDLYRSQKRG
GKGVQGAGLK QDDIVAHFFV CSTHDLILFF TTQGRVYRAK AYDLPEASRT ARGQHVANLL
AFQPEERIAQ VIQIRGYTDA PYLVLATRNG LVKKSKLTDF DSNRSGGIVA VNLRDNDELV
GAVLCSADDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG
TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG
GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN
