ID A0A2R4IPV2_MYCTX Unreviewed; 838 AA. AC A0A2R4IPV2; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 03-AUG-2022, entry version 15. DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897}; DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897, GN ECO:0000313|EMBL:AVV29465.1}; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773 {ECO:0000313|EMBL:AVV29465.1}; RN [1] {ECO:0000313|EMBL:AVV29465.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UKR43 {ECO:0000313|EMBL:AVV29465.1}; RA Daum L.T., Rodriguez J.D.; RT "Next-Generation Sequencing for Characterizing Drug Resistance-Conferring RT Mycobacterium tuberculosis Genes from Clinical Isolates in the Ukraine."; RL J. Clin. Microbiol. 0:0-0(2018). 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:0000256|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:0000256|ARBA:ARBA00000185, CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. {ECO:0000256|ARBA:ARBA00008263}. 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; MG995144; AVV29465.1; -; Genomic_DNA. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01897}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01897}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01897}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_01897}. FT DOMAIN 18..476 FT /note="TOP4c" FT /evidence="ECO:0000259|SMART:SM00434" FT COILED 448..475 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 537..543 FT /note="GyrA-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897" FT ACT_SITE 129 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897" SQ SEQUENCE 838 AA; 92328 MW; 8E7E5862F911E1FE CRC64; MTDTTLPPDD SLDRIEPVDI QQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF DSGFRPDRSH AKSARSVAET MGNYHPHGDX SIYGTLVRMA QPWSLRYPLV DGQGNFGSPG NDPPAAMRYT EARLTPLAME MLREIDEETV DFIPNYDGRV QEPTVLPSRF PNLLANGSGG IAVGMATNIP PHNLRELADA VFWALENHDA DEEETLAAVM GRVKGPDFPT AGLIVGSQGT ADAYKTGRGS IRMRGVVEVE EDSRGRTSLV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS NIEDQSSDRV GLRIVIEIKR DAVAKVVINN LYKHTQLQTS FGANMLAIVD GVPRTLRLDQ LIRYYVDHQL DVIVRRTTYR LRKANERAHI LRGLVKALDA LDEVIALIRA SETVDIARAG LIELLDIDEI QAQAILDMQL RRLAALERQR IIDDLAKIEA EIADLEDILA KPERQRGIVR DELAEIVDRH GDDRRTRIIA ADGDVSDEDL IAREDVVVTI TETGYAKRTK TDLYRSQKRG GKGVQGAGLK QDDIVAHFFV CSTHDLILFF TTQGRVYRAK AYDLPEASRT ARGQHVANLL AFQPEERIAQ VIQIRGYTDA PYLVLATRNG LVKKSKLTDF DSNRSGGIVA VNLRDNDELV GAVLCSADDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN //