ID GYRA_MYCTU Reviewed; 838 AA. AC P9WG47; J9VB15; P71574; P97136; Q07702; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 24-JUN-2015, entry version 14. DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=Rv0006; GN ORFNames=MTCY10H4.04; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=8031045; DOI=10.1128/AAC.38.4.773; RA Takiff H.E., Salazar L., Guerrero C., Philipp W., Huang W.M., RA Kreiswirth B., Cole S.T., Jacobs W.R. Jr., Telenti A.; RT "Cloning and nucleotide sequence of Mycobacterium tuberculosis gyrA RT and gyrB genes and detection of quinolone resistance mutations."; RL Antimicrob. Agents Chemother. 38:773-780(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=2997164; RX PubMed=22972833; DOI=10.1128/JCM.01893-12; RA Daum L.T., Rodriguez J.D., Worthy S.A., Ismail N.A., Omar S.V., RA Dreyer A.W., Fourie P.B., Hoosen A.A., Chambers J.P., Fischer G.W.; RT "Next-generation ion torrent sequencing of drug resistance mutations RT in Mycobacterium tuberculosis strains."; RL J. Clin. Microbiol. 50:3831-3837(2012). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-188. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=8294019; DOI=10.1016/0378-1119(93)90481-H; RA Mizrahi V., Huberts P., Dawes S.S., Dudding L.R.; RT "A PCR method for the sequence analysis of the gyrA, polA and rnhA RT gene segments from mycobacteria."; RL Gene 136:287-290(1993). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-124. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=8035042; RA Cambau E., Sougakoff W., Besson M., Truffot-Pernot C., Grosset J., RA Jarlier V.; RT "Selection of a gyrA mutant of Mycobacterium tuberculosis resistant to RT fluoroquinolones during treatment with ofloxacin."; RL J. Infect. Dis. 170:479-483(1994). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.M111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double- CC stranded DNA in an ATP-dependent manner and also catalyzes the CC interconversion of other topological isomers of double-stranded CC DNA rings, including catenanes and knotted rings. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC Within the heterotetramer, GyrA contains the active site tyrosine CC that forms a covalent intermediate with the DNA, while GyrB CC contributes the cofactor binding sites and catalyzes ATP CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- MISCELLANEOUS: When the enzyme transiently cleaves DNA a CC phosphotyrosine bond is formed between the gyrA and DNA. CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family. CC {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; L27512; AAA83017.1; -; Genomic_DNA. DR EMBL; JX303241; AFR90330.1; -; Genomic_DNA. DR EMBL; AL123456; CCP42728.1; -; Genomic_DNA. DR EMBL; L11919; AAC36878.1; -; Unassigned_DNA. DR EMBL; X72872; CAA51386.1; -; Genomic_DNA. DR PIR; D70698; D70698. DR RefSeq; NP_214520.1; NC_000962.3. DR RefSeq; WP_003917265.1; NZ_KK339370.1. DR RefSeq; YP_006513318.1; NC_018143.2. DR PDB; 3IFZ; X-ray; 2.70 A; A/B=1-501. DR PDB; 3ILW; X-ray; 1.60 A; A/B=34-500. DR PDB; 3UC1; X-ray; 1.65 A; A=514-838. DR PDB; 4G3N; X-ray; 1.40 A; A=512-838. DR PDBsum; 3IFZ; -. DR PDBsum; 3ILW; -. DR PDBsum; 3UC1; -. DR PDBsum; 4G3N; -. DR ProteinModelPortal; P9WG47; -. DR SMR; P9WG47; 9-501, 512-820. DR ChEMBL; CHEMBL4165; -. DR EnsemblBacteria; CCP42728; CCP42728; Rv0006. DR GeneID; 887105; -. DR KEGG; mtu:Rv0006; -. DR KEGG; mtv:RVBD_0006; -. DR TubercuList; Rv0006; -. DR KO; K02469; -. DR PhylomeDB; P9WG47; -. DR PRO; PR:P9WG47; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005618; C:cell wall; IDA:MTBBASE. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE. DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:MTBBASE. DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE. DR GO; GO:0006265; P:DNA topological change; IDA:MTBBASE. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_01897; GyrA; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR005743; GyrA. DR InterPro; IPR006691; GyrA/parC_pinwhl. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013760; Topo_IIA_like_dom. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Antibiotic resistance; ATP-binding; KW Complete proteome; Cytoplasm; DNA-binding; Isomerase; KW Nucleotide-binding; Reference proteome; Topoisomerase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:21969609}. FT CHAIN 2 838 DNA gyrase subunit A. FT /FTId=PRO_0000145243. FT ACT_SITE 129 129 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01897}. FT MOD_RES 2 2 N-acetylthreonine. FT {ECO:0000269|PubMed:21969609}. FT VARIANT 88 88 G -> C (confers ciprofloxacin FT resistance). FT VARIANT 90 90 A -> V (confers ciprofloxacin FT resistance). FT VARIANT 91 91 S -> P (confers ciprofloxacin FT resistance). FT VARIANT 94 94 D -> A (confers ciprofloxacin FT resistance). FT VARIANT 94 94 D -> G (confers ciprofloxacin FT resistance). FT VARIANT 94 94 D -> H (confers ciprofloxacin FT resistance). FT VARIANT 94 94 D -> N (confers ciprofloxacin FT resistance). FT VARIANT 94 94 D -> Y (confers ciprofloxacin FT resistance). FT VARIANT 95 95 S -> T. FT CONFLICT 83 83 N -> K (in Ref. 4; AAC36878). FT {ECO:0000305}. FT CONFLICT 712 712 L -> V (in Ref. 1; AAA83017). FT {ECO:0000305}. FT TURN 38 40 {ECO:0000244|PDB:3ILW}. FT TURN 44 46 {ECO:0000244|PDB:3ILW}. FT HELIX 50 62 {ECO:0000244|PDB:3ILW}. FT HELIX 73 83 {ECO:0000244|PDB:3ILW}. FT HELIX 91 100 {ECO:0000244|PDB:3ILW}. FT TURN 102 104 {ECO:0000244|PDB:3ILW}. FT STRAND 109 114 {ECO:0000244|PDB:3ILW}. FT STRAND 119 121 {ECO:0000244|PDB:3ILW}. FT TURN 127 129 {ECO:0000244|PDB:3IFZ}. FT STRAND 131 134 {ECO:0000244|PDB:3ILW}. FT HELIX 136 142 {ECO:0000244|PDB:3ILW}. FT HELIX 145 147 {ECO:0000244|PDB:3ILW}. FT STRAND 152 154 {ECO:0000244|PDB:3ILW}. FT STRAND 158 165 {ECO:0000244|PDB:3ILW}. FT HELIX 172 176 {ECO:0000244|PDB:3ILW}. FT STRAND 178 184 {ECO:0000244|PDB:3IFZ}. FT STRAND 186 189 {ECO:0000244|PDB:3IFZ}. FT HELIX 194 206 {ECO:0000244|PDB:3ILW}. FT TURN 207 209 {ECO:0000244|PDB:3ILW}. FT HELIX 212 222 {ECO:0000244|PDB:3ILW}. FT STRAND 233 235 {ECO:0000244|PDB:3ILW}. FT HELIX 238 246 {ECO:0000244|PDB:3ILW}. FT STRAND 247 254 {ECO:0000244|PDB:3ILW}. FT STRAND 256 261 {ECO:0000244|PDB:3ILW}. FT STRAND 267 273 {ECO:0000244|PDB:3ILW}. FT HELIX 280 292 {ECO:0000244|PDB:3ILW}. FT STRAND 299 304 {ECO:0000244|PDB:3ILW}. FT TURN 308 310 {ECO:0000244|PDB:3ILW}. FT STRAND 314 318 {ECO:0000244|PDB:3ILW}. FT HELIX 324 334 {ECO:0000244|PDB:3ILW}. FT STRAND 338 344 {ECO:0000244|PDB:3ILW}. FT STRAND 346 349 {ECO:0000244|PDB:3ILW}. FT STRAND 352 355 {ECO:0000244|PDB:3ILW}. FT HELIX 358 399 {ECO:0000244|PDB:3ILW}. FT HELIX 401 410 {ECO:0000244|PDB:3ILW}. FT HELIX 414 425 {ECO:0000244|PDB:3ILW}. FT HELIX 429 436 {ECO:0000244|PDB:3ILW}. FT HELIX 440 443 {ECO:0000244|PDB:3ILW}. FT HELIX 445 470 {ECO:0000244|PDB:3ILW}. FT HELIX 472 490 {ECO:0000244|PDB:3ILW}. FT STRAND 496 499 {ECO:0000244|PDB:3ILW}. FT STRAND 515 521 {ECO:0000244|PDB:4G3N}. FT STRAND 524 530 {ECO:0000244|PDB:4G3N}. FT HELIX 531 534 {ECO:0000244|PDB:4G3N}. FT HELIX 551 553 {ECO:0000244|PDB:4G3N}. FT STRAND 555 562 {ECO:0000244|PDB:4G3N}. FT STRAND 565 571 {ECO:0000244|PDB:4G3N}. FT STRAND 574 580 {ECO:0000244|PDB:4G3N}. FT HELIX 581 583 {ECO:0000244|PDB:4G3N}. FT STRAND 589 591 {ECO:0000244|PDB:3UC1}. FT HELIX 596 599 {ECO:0000244|PDB:4G3N}. FT STRAND 608 616 {ECO:0000244|PDB:4G3N}. FT STRAND 619 627 {ECO:0000244|PDB:4G3N}. FT STRAND 630 636 {ECO:0000244|PDB:4G3N}. FT HELIX 637 640 {ECO:0000244|PDB:4G3N}. FT STRAND 645 650 {ECO:0000244|PDB:4G3N}. FT STRAND 659 665 {ECO:0000244|PDB:4G3N}. FT STRAND 670 675 {ECO:0000244|PDB:4G3N}. FT STRAND 678 684 {ECO:0000244|PDB:4G3N}. FT TURN 687 689 {ECO:0000244|PDB:4G3N}. FT STRAND 695 697 {ECO:0000244|PDB:4G3N}. FT STRAND 700 702 {ECO:0000244|PDB:4G3N}. FT STRAND 711 716 {ECO:0000244|PDB:4G3N}. FT STRAND 722 727 {ECO:0000244|PDB:4G3N}. FT STRAND 730 736 {ECO:0000244|PDB:4G3N}. FT HELIX 737 739 {ECO:0000244|PDB:4G3N}. FT STRAND 750 753 {ECO:0000244|PDB:4G3N}. FT TURN 757 759 {ECO:0000244|PDB:4G3N}. FT STRAND 762 768 {ECO:0000244|PDB:4G3N}. FT STRAND 773 781 {ECO:0000244|PDB:4G3N}. FT STRAND 783 787 {ECO:0000244|PDB:4G3N}. FT HELIX 788 790 {ECO:0000244|PDB:4G3N}. FT STRAND 812 818 {ECO:0000244|PDB:4G3N}. SQ SEQUENCE 838 AA; 92274 MW; 84DAFE13D74D76D7 CRC64; MTDTTLPPDD SLDRIEPVDI EQEMQRSYID YAMSVIVGRA LPEVRDGLKP VHRRVLYAMF DSGFRPDRSH AKSARSVAET MGNYHPHGDA SIYDSLVRMA 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 GAVLCSAGDD LLLVSANGQS IRFSATDEAL RPMGRATSGV QGMRFNIDDR LLSLNVVREG TYLLVATSGG YAKRTAIEEY PVQGRGGKGV LTVMYDRRRG RLVGALIVDD DSELYAVTSG GGVIRTAARQ VRKAGRQTKG VRLMNLGEGD TLLAIARNAE ESGDDNAVDA NGADQTGN //