ID Q9HR29_HALSA Unreviewed; 824 AA. AC Q9HR29; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 01-OCT-2014, entry version 82. DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897, GN ECO:0000313|EMBL:AAG19329.1}; GN OrderedLocusNames=VNG_0889G {ECO:0000313|EMBL:AAG19329.1}; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG19329.1, ECO:0000313|Proteomes:UP000000554}; RN [1] {ECO:0000313|EMBL:AAG19329.1, ECO:0000313|Proteomes:UP000000554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1 RC {ECO:0000313|Proteomes:UP000000554}; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., RA Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., RA Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., RA Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W., RA Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., RA Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., RA Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., RA Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). 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 {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family. CC {ECO:0000256|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; AE004437; AAG19329.1; -; Genomic_DNA. DR PIR; E84245; E84245. DR RefSeq; NP_279849.1; NC_002607.1. DR RefSeq; WP_010902625.1; NC_002607.1. DR ProteinModelPortal; Q9HR29; -. DR STRING; 64091.VNG0889G; -. DR PaxDb; Q9HR29; -. DR PRIDE; Q9HR29; -. DR EnsemblBacteria; AAG19329; AAG19329; VNG_0889G. DR GeneID; 1447633; -. DR KEGG; hal:VNG0889G; -. DR eggNOG; COG0188; -. DR KO; K02469; -. DR OMA; AITFEIA; -. DR PhylomeDB; Q9HR29; -. 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-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897}; KW Complete proteome {ECO:0000313|Proteomes:UP000000554}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01897}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897}; KW Reference proteome {ECO:0000313|Proteomes:UP000000554}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897}. FT ACT_SITE 130 130 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01897}. SQ SEQUENCE 824 AA; 90223 MW; CB55755219FE09F0 CRC64; MSSESPDVPD DVADRVKNVR VDEEMEQSYI DYAMSVIAGR ALPDVRDGLK PVHRRILYAM HESGVTSGSG HRKSSNIVGD TMGDYHPHGD SPIYDALVRM AQDFSMRYPL VDGQGNFGSV DGDPAAAMRY TEARMAPIAE ELLTDIEKDT VAFQANYDDR LTEPAVLPSS FPNLLVNGSS GIAVGMSTNV PPHNLGEVID ATIHLIDTPD CTVLDLMEYV KGPDFPTAAN IVGRADVKQA YQTGRGRVRM RAEYHVESNG RRDSIVITEL PYQQNKSTLV ERIADDVRDG KLEGITDLRD ESDRNGVRIV IDLKQKANTD VVENRLLESH LEKTFSVINL ALVDGEPKVL TLKELLAEYV SHRKEVVRRR SEHDLGEAED RAHILDGRLT ALENADEVVE LIQDAEDRDA AKETLKSAFD FSQDQADHIV RMQLGSLTSM EAADIESEYE DVTARIERLE EILGSEQELL DVIKDELREI KTQYADERRT SFIEDTGTVA DEDLIPEEDT VVVLSEGDYI KRVPAETFDA QHRGGKGIIG SDLKDGDRVS TVFTASTHDY LLCFTDQGQV YRLKVYQVPE MSRTARGTSA VNILDLDDGE EISAVVTADD LDFKADDEYL TMATRNGYVK RTSVGEFGNI LSTGIIAIDL EDGDALADVE VTDGSHDVIL GSEAGMAIRF DEGDVRAMGR NARGVRGMDL DAADRIAGVA AVESEDDRSL LTVTEFGYGK RTRVGEYRSQ SRNGKGLVDI KTGDRNGDVV SVDAVGDDDS LVVMSADGQI IQMPVDEIST VGRNTKGVNI MAVGSGDEVA GVSVRAADQA DGEE //