ID GYRA_MYCXE Reviewed; 327 AA. AC P72065; P95323; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 27-MAR-2024, entry version 127. DE RecName: Full=DNA gyrase subunit A; DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU01384}; DE Contains: DE RecName: Full=Mxe GyrA intein; DE Flags: Fragment; GN Name=gyrA; OS Mycobacterium xenopi. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1789; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IMM 5024; RX PubMed=9335286; DOI=10.1128/jb.179.20.6378-6382.1997; RA Telenti A., Southworth M., Alcaide F., Daugelat S., Jacobs W.R. Jr., RA Perler F.B.; RT "The Mycobacterium xenopi GyrA protein splicing element: characterization RT of a minimal intein."; RL J. Bacteriol. 179:6378-6382(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INTEIN. RX PubMed=9437427; DOI=10.1038/nsb0198-31; RA Klabunde T., Sharma S., Telenti A., Jacobs W.R. Jr., Sacchettini J.C.; RT "Crystal structure of GyrA intein from Mycobacterium xenopi reveals RT structural basis of protein splicing."; RL Nat. Struct. Biol. 5:31-36(1998). 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. CC {ECO:0000250|UniProtKB:P0AES4}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01384}; 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:0000250|UniProtKB:P0AES4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AES4}. CC -!- PTM: This protein undergoes a protein self splicing that involves a CC post-translational excision of the intervening region (intein) followed CC by peptide ligation. {ECO:0000305|PubMed:9437427}. 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. CC {ECO:0000250|UniProtKB:P0AES4}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. 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; U67876; AAB81424.1; -; Genomic_DNA. DR PDB; 1AM2; X-ray; 2.20 A; A=67-263. DR PDB; 4OZ6; X-ray; 2.79 A; A=66-267, B=62-65. DR PDBsum; 1AM2; -. DR PDBsum; 4OZ6; -. DR AlphaFoldDB; P72065; -. DR SMR; P72065; -. DR MEROPS; N10.008; -. DR EvolutionaryTrace; P72065; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR CDD; cd00081; Hint; 1. DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1. DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 2. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR036844; Hint_dom_sf. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR002205; Topo_IIA_dom_A. DR NCBIfam; TIGR01443; intein_Cterm; 1. DR NCBIfam; TIGR01445; intein_Nterm; 1. DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1. DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1. DR Pfam; PF00521; DNA_topoisoIV; 2. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 2. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS52040; TOPO_IIA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA-binding; KW Isomerase; Nucleotide-binding; Protein splicing; Topoisomerase. FT CHAIN <1..65 FT /note="DNA gyrase subunit A, 1st part" FT /id="PRO_0000034813" FT CHAIN 66..263 FT /note="Mxe GyrA intein" FT /id="PRO_0000034814" FT CHAIN 264..>327 FT /note="DNA gyrase subunit A, 2nd part" FT /id="PRO_0000034815" FT DOMAIN 1..327 FT /note="Topo IIA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" FT ACT_SITE 65 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" FT NON_TER 1 FT NON_TER 327 FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1AM2" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 94..103 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 109..128 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:1AM2" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:1AM2" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:1AM2" FT HELIX 201..207 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:1AM2" FT HELIX 214..222 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 226..251 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:1AM2" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:1AM2" SQ SEQUENCE 327 AA; 35386 MW; EFAE9924D97068FB CRC64; RPDRSHAKSA RSVAETMGNY HPHGDASIYD TLVRMAQPWS MRYPLVDGQG NFGSPGNDPP AAMRYCITGD ALVALPEGES VRIADIVPGA RPNSDNAIDL KVLDRHGNPV LADRLFHSGE HPVYTVRTVE GLRVTGTANH PLLCLVDVAG VPTLLWKLID EIKPGDYAVI QRSAFSVDCA GFARGKPEFA PTTYTVGVPG LVRFLEAHHR DPDAQAIADE LTDGRFYYAK VASVTDAGVQ PVYSLRVDTA DHAFITNGFV SHNTEAPLTP LAMEMLREID EETVDFIPNY DGRVQEPTVL PSRFPNLLAN GSGGIAVGMA TNIPPHN //