ID GYRA_SHIFL Reviewed; 875 AA. AC P0AES5; P09097; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 138. 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=SF2311, S2444; OS Shigella flexneri. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(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}. 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; AE005674; AAN43827.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17645.1; -; Genomic_DNA. DR RefSeq; NP_708120.1; NC_004337.2. DR RefSeq; WP_001281242.1; NZ_AP040250.1. DR PDB; 2Y3P; X-ray; 2.62 A; A/B=2-523. DR AlphaFoldDB; P0AES5; -. DR MDRepo; P0AES5; -. DR SMR; P0AES5; -. DR STRING; 198214.SF2311; -. DR PaxDb; 198214-SF2311; -. DR GeneID; 1027274; -. DR GeneID; 75206476; -. DR KEGG; sfl:SF2311; -. DR KEGG; sfx:S2444; -. DR PATRIC; fig|198214.7.peg.2769; -. DR HOGENOM; CLU_002977_6_1_6; -. DR EvolutionaryTrace; P0AES5; -. DR Proteomes; UP000001006; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:TreeGrafter. 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:UniProtKB-ARBA. 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 FunFam; 2.120.10.90:FF:000002; DNA gyrase subunit A; 1. DR FunFam; 3.30.1360.40:FF:000002; 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; TIGR01063; gyrA; 1. DR NCBIfam; NF004043; PRK05560.1; 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. DR PDBsum; 2Y3P; -. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; KW Isomerase; Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1..875 FT /note="DNA gyrase subunit A" FT /id="PRO_0000145249" FT DOMAIN 34..533 FT /note="Topo IIA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" FT REGION 841..875 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 560..566 FT /note="GyrA-box" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897" FT COMPBIAS 857..875 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 122 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 24..33 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 43..54 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 66..76 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 84..91 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 135..139 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 165..169 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 174..177 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 187..199 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 205..211 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 227..235 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 236..243 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 270..282 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 303..307 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 313..321 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 327..333 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 335..338 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 347..388 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 390..399 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 403..412 FT /evidence="ECO:0007829|PDB:2Y3P" FT TURN 418..420 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 421..424 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 441..449 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 452..460 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 463..466 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 469..492 FT /evidence="ECO:0007829|PDB:2Y3P" FT HELIX 495..513 FT /evidence="ECO:0007829|PDB:2Y3P" FT STRAND 519..521 FT /evidence="ECO:0007829|PDB:2Y3P" SQ SEQUENCE 875 AA; 96964 MW; 3FD5BD52A5969069 CRC64; MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE //