GYRA_STRPN
ID GYRA_STRPN Reviewed; 822 AA.
AC P72524; P72536; Q54716;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 144.
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=SP_1219;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-120.
RC STRAIN=NCTC 7465;
RA Jin Y.F., Everett M.J., Piddock L.J.V.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-108.
RC STRAIN=BM4203;
RA Tankovic J., Perichon B., Courvalin P.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
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; AE005672; AAK75325.1; -; Genomic_DNA.
DR EMBL; U37560; AAA79196.1; -; Genomic_DNA.
DR EMBL; U49087; AAB08037.1; -; Genomic_DNA.
DR PIR; D95141; D95141.
DR RefSeq; WP_001152989.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P72524; -.
DR SMR; P72524; -.
DR STRING; 170187.SP_1219; -.
DR ChEMBL; CHEMBL2311225; -.
DR DrugBank; DB06771; Besifloxacin.
DR DrugBank; DB01044; Gatifloxacin.
DR DrugCentral; P72524; -.
DR EnsemblBacteria; AAK75325; AAK75325; SP_1219.
DR KEGG; spn:SP_1219; -.
DR eggNOG; COG0188; Bacteria.
DR OMA; THHWLLF; -.
DR PhylomeDB; P72524; -.
DR BioCyc; SPNE170187:G1FZB-1233-MON; -.
DR PRO; PR:P72524; -.
DR Proteomes; UP000000585; 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..822
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145262"
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 822 AA; 92053 MW; D24F7C56FCBCD70A CRC64;
MQDKNLVNVN LTKEMKASFI DYAMSVIVAR ALPDVRDGLK PVHRRILYGM NELGVTPDKP
HKKSARITGD VMGKYHPHGD SSIYEAMVRM AQWWSYRYML VDGHGNFGSM DGDSAAAQRY
TEARMSKIAL EMLRDINKNT VDFVDNYDAN EREPLVLPAR FPNLLVNGAT GIAVGMATNI
PPHNLGETID AVKLVMDNPE VTTKDLMEVL PGPDFPTGAL VMGKSGIHKA YETGKGSIVL
RSRTEIETTK TGRERIVVTE FPYMVNKTKV HEHIVRLVQE KRIEGITAVR DESNREGVRF
VIEVKRDASA NVILNNLFKM TQMQTNFGFN MLAIQNGIPK ILSLRQILDA YIEHQKEVVV
RRTRFDKEKA EARAHILEGL LIALDHIDEV IRIIRASETD AEAQAELMSK FKLSERQSQA
ILDMRLRRLT GLERDKIQSE YDDLLALIAD LADILAKPER VSQIIKDELD EVKRKFSDKR
RTELMIGQVL SLEDEDLIEE SDVLITLSNR GYIKRLDQDE FTAQKRGGRG VQGTGVKDDD
FVRELVSTST HDHLLFFTNK GRVYRLKGYE IPEYGRTAKG LPVVNLLKLD EDESIQTVIN
VESDRSDDAY LFFTTRHGIV KRTSVKEFAN IRQNGLKALN LKDEDELINV LLAEGDMDII
IGTKFGYAVR FNQSAVRGMS RIATGVKGVN LREGDTVVGA SLITDQDEVL IITEKGYGKR
TVATEYPTKG RGGKGMQTAK ITEKNGLLAG LMTVQGDEDL MIITDTGVMI RTNLANISQT
GRATMGVKVM RLDQDAQIVT FTTVAVAEKE EVGTENETEG EA