ID GYRA_STRR6 Reviewed; 822 AA. AC Q8DPM2; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 04-NOV-2026, entry version 135. 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}; GN OrderedLocusNames=spr1099; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9603872; DOI=10.1128/jb.180.11.2854-2861.1998; RA Balas D., Fernandez-Moreira E., de la Campa A.G.; RT "Molecular characterization of the gene encoding the DNA gyrase A subunit RT of Streptococcus pneumoniae."; RL J. Bacteriol. 180:2854-2861(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-145. RA Janoir C.; RL Submitted (SEP-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF053121; AAC23563.1; -; Genomic_DNA. DR EMBL; AE007317; AAK99902.1; -; Genomic_DNA. DR EMBL; Y07845; CAA69173.1; -; Genomic_DNA. DR PIR; B98009; B98009. DR RefSeq; WP_001152994.1; NC_003098.1. DR PDB; 4Z2C; X-ray; 3.19 A; A/B=1-493. DR PDB; 4Z2D; X-ray; 3.38 A; A/B=1-493. DR PDB; 4Z2E; X-ray; 3.46 A; A/B=1-493. DR PDB; 6N1P; EM; 6.35 A; A/B/C/D/E/F/G/H=1-487. DR PDB; 6N1Q; EM; 5.16 A; A/B/C/D/E/F/G/H=1-487. DR PDB; 6N1R; EM; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-487. DR AlphaFoldDB; Q8DPM2; -. DR SMR; Q8DPM2; -. DR STRING; 171101.spr1099; -. DR PaxDb; 171101-spr1099; -. DR KEGG; spr:spr1099; -. DR PATRIC; fig|171101.6.peg.1194; -. DR eggNOG; COG0188; Bacteria. DR HOGENOM; CLU_002977_6_1_9; -. DR OMA; AACHIEN; -. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProtKB-ARBA. DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd00187; TOP4c; 1. DR FunFam; 1.10.268.10:FF:000001; DNA gyrase subunit A; 1. DR FunFam; 2.120.10.90:FF:000004; DNA gyrase subunit A; 1. DR FunFam; 3.90.199.10:FF:000001; DNA gyrase subunit A; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1. DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1. DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 InterPro; IPR050220; Type_II_DNA_Topoisomerases. DR NCBIfam; NF004043; gyrA; 1. DR NCBIfam; TIGR01063; gyrA; 1. DR NCBIfam; NF004044; PRK05561.1; 1. DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1. DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS52040; TOPO_IIA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; DNA-binding; Isomerase; KW Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1..822 FT /note="DNA gyrase subunit A" FT /id="PRO_0000145263" FT DOMAIN 32..497 FT /note="Topo IIA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" 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" FT CONFLICT 537 FT /note="K -> E (in Ref. 1; AAC23563)" FT /evidence="ECO:0000305" FT CONFLICT 618..620 FT /note="GIV -> VLL (in Ref. 1; AAC23563)" FT /evidence="ECO:0000305" FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 11..26 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 27..31 FT /evidence="ECO:0007829|PDB:4Z2C" FT TURN 35..38 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 41..53 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 64..70 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 80..89 FT /evidence="ECO:0007829|PDB:4Z2C" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 113..117 FT /evidence="ECO:0007829|PDB:4Z2C" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 129..133 FT /evidence="ECO:0007829|PDB:4Z2C" FT TURN 134..139 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 185..197 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 203..207 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 234..241 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:4Z2E" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 267..278 FT /evidence="ECO:0007829|PDB:4Z2C" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 310..320 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 324..330 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 344..385 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 387..395 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 400..411 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 415..422 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 433..456 FT /evidence="ECO:0007829|PDB:4Z2C" FT HELIX 458..476 FT /evidence="ECO:0007829|PDB:4Z2C" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:4Z2C" SQ SEQUENCE 822 AA; 92039 MW; 130307B8B5160EAD 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 RTELMVGQVL 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 //