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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
 
 
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