GYRA_STRP8
ID GYRA_STRP8 Reviewed; 828 AA.
AC Q8P116;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=spyM18_1112;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97734.1; -; Genomic_DNA.
DR RefSeq; WP_011017764.1; NC_003485.1.
DR AlphaFoldDB; Q8P116; -.
DR SMR; Q8P116; -.
DR KEGG; spm:spyM18_1112; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
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..828
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145267"
FT MOTIF 524..530
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 828 AA; 92744 MW; 1B0EC71B282E37BA CRC64;
MQDRNLIDVN LTSEMKTSFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRHML VDGHGNFGSM DGDGAAAQRY
TEARMSKIAL ELLRDINKNT VNFQDNYDGS EREPVVLPAR FPNLLVNGAT GIAVGMATNI
PPHNLAESID AVKMVMEHPD CTTRELMEVI PGPDFPTGAL VMGRSGIHRA YDTGKGSIVL
RSRTEIETTQ TGRERIVVTE FPYGVNKTKV HEHIVRLAQE KRLEGITAVR DESSREGVRF
VIEIRREASA TVILNNLFKL TSLQTNFSFN MLAIENGVPK ILSLRQIIDN YISYQKEVII
RRTRFDKDKA EARAHILEGL LIALDHLDEV IAIIRNSETD VIAQTELMSR FDLSERQSQA
ILDMRLRRLT GLERDKIQSE YDDLLALIAD LSDILAKPER IITIIKEEMD EIKRKYANPR
RTELMVGEVL SLEDEDLIEE EDVLITLSNK GYIKRLAQDE FRAQKRGGRG VQGTGVNNDD
FVRELVSTST HDTLLFFTNF GRVYRLKAYE IPEYGRTAKG LPIVNLLKLE DGETIQTIIN
ARKEETAGKS FFFTTKQGIV KRTEVSEFNN IRQNGLRALK LKEGDQLINV LLTSGQDDII
IGTHSGYSVR FNEASIRNMG RSATGVRGVK LREDDRVVGA SRIRDNQEVL VITENGFGKR
TSATDYPTKG RGGKGIKTAN ITPKNGQLAG LVTVDGTEDI MVITNKGVII RTNVANISQT
GRATLGVKIM KLDADAKIVT FTLVQPEDSS IAEINTDREN SISKNKDN