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 29-OCT-2014, entry version 7. 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; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC 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; NC_018143.2. 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 GeneID; 13315979; -. DR GeneID; 887105; -. DR KEGG; mtu:Rv0006; -. DR KEGG; mtv:RVBD_0006; -. DR TubercuList; Rv0006; -. DR KO; K02469; -. DR PhylomeDB; P9WG47; -. 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-HAMAP. 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:0046982; F:protein heterodimerization activity; IPI:MTBBASE. DR GO; GO:0006200; P:ATP catabolic process; 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 FT TURN 44 46 FT HELIX 50 62 FT HELIX 73 83 FT HELIX 91 100 FT TURN 102 104 FT STRAND 109 114 FT STRAND 119 121 FT TURN 127 129 FT STRAND 131 134 FT HELIX 136 142 FT HELIX 145 147 FT STRAND 152 154 FT STRAND 158 165 FT HELIX 172 176 FT STRAND 178 184 FT STRAND 186 189 FT HELIX 194 206 FT TURN 207 209 FT HELIX 212 222 FT STRAND 233 235 FT HELIX 238 246 FT STRAND 247 254 FT STRAND 256 261 FT STRAND 267 273 FT HELIX 280 292 FT STRAND 299 304 FT TURN 308 310 FT STRAND 314 318 FT HELIX 324 334 FT STRAND 338 344 FT STRAND 346 349 FT STRAND 352 355 FT HELIX 358 399 FT HELIX 401 410 FT HELIX 414 425 FT HELIX 429 436 FT HELIX 440 443 FT HELIX 445 470 FT HELIX 472 490 FT STRAND 496 499 FT STRAND 515 521 FT STRAND 524 530 FT HELIX 531 534 FT HELIX 551 553 FT STRAND 555 562 FT STRAND 565 571 FT STRAND 574 580 FT HELIX 581 583 FT STRAND 589 591 FT HELIX 596 599 FT STRAND 608 616 FT STRAND 619 627 FT STRAND 630 636 FT HELIX 637 640 FT STRAND 645 650 FT STRAND 659 665 FT STRAND 670 675 FT STRAND 678 684 FT TURN 687 689 FT STRAND 695 697 FT STRAND 700 702 FT STRAND 711 716 FT STRAND 722 727 FT STRAND 730 736 FT HELIX 737 739 FT STRAND 750 753 FT TURN 757 759 FT STRAND 762 768 FT STRAND 773 781 FT STRAND 783 787 FT HELIX 788 790 FT STRAND 812 818 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 //