GYRA_STAES
ID GYRA_STAES Reviewed; 893 AA.
AC P0C0R0; P54112;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=SE_0005;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
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 -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
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; AE015929; AAO03602.1; -; Genomic_DNA.
DR RefSeq; NP_763560.1; NC_004461.1.
DR RefSeq; WP_001831812.1; NZ_WBME01000012.1.
DR AlphaFoldDB; P0C0R0; -.
DR SMR; P0C0R0; -.
DR STRING; 176280.SE_0005; -.
DR EnsemblBacteria; AAO03602; AAO03602; SE_0005.
DR GeneID; 50017420; -.
DR KEGG; sep:SE_0005; -.
DR PATRIC; fig|176280.10.peg.6; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000001411; 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; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Topoisomerase.
FT CHAIN 1..893
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145259"
FT REGION 810..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 528..534
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 852..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 893 AA; 100114 MW; 2A6A7CD345A526CE CRC64;
MAELPQSRIN ERNITSEMRE SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YGLNEQGMTP
DKPYKKSARI VGDVMGKYHP HGDSSIYEAM VRMAQDFSYR YPLVDGQGNF GSMDGDGAAA
MRYTEARMTK ITLELLRDIN KDTIDFIDNY DGNEREPSVL PARFPNLLVN GAAGIAVGMA
TNIPPHNLTE VIDGVLSLSK NPDITINELM EDIQGPDFPT AGLVLGKSGI RRAYETGRGS
IQMRSRAEIE ERGGGRQRIV VTEIPFQVNK ARMIEKIAEL VRDKKIDGIT DLRDETSLRT
GVRVVIDVRK DANASVILNN LYKQTPLQTS FGVNMIALVN GRPKLINLKE ALIHYLEHQK
TVVRRRTEYN LKKARDRAHI LEGLRIALDH IDEIITTIRE SDTDKIAMAS LQERFKLTER
QAQAILDMRL RRLTGLERDK IESEYNELLE YIKELEEILA DEEVLLQLVR DELTEIKERF
GDERRTEIQL GGLEDLEDED LIPEEQIVIT LSHNNYIKRL PVSTYRSQNR GGRGIQGMNT
LDEDFVSQLV TMSTHDHVLF FTNKGRVYKL KGYEVPELSR QSKGIPIINA IELENDETIS
TMIAVKDLES EEDYLVFATK QGIVKRSSLS NFSRINKNGK IAINFKEDDE LIAVRLTTGN
EDILIGTAHA SLIRFSESTL RPLGRTAAGV KGISLREGDT VVGLDVADSE SEDEVLVVTE
NGYGKRTPVS EYRLSNRGGK GIKTATITER NGNIVCITTV TGEEDLMVVT NAGVIIRLDV
HDISQNGRAA QGVRLMKLGD GQFVSTVAKV NEEDDNEENA DEAQQSTTTE TADVEEVVDD
QTPGNAIHTE GDAEMESVES PENDDRIDIR QDFMDRVNED IESASDNEED SDE
