ID Q9HR29_HALSA Unreviewed; 824 AA. AC Q9HR29; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 16-OCT-2019, entry version 117. 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: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; Stenosarchaea group; Halobacteria; OC Halobacteriales; 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}, and NRC-1 RC {ECO:0000313|EMBL:AAG19329.1}; 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.W., 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). RN [2] {ECO:0000313|EMBL:DAC78034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78034.1}; RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001; RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., RA Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.; RT "Evolution in the laboratory: the genome of Halobacterium salinarum RT strain R1 compared to that of strain NRC-1."; RL Genomics 91:335-346(2008). RN [3] {ECO:0000313|EMBL:DAC78034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78034.1}; RX PubMed=26042526; RA Pfeiffer F., Oesterhelt D.; RT "A manual curation strategy to improve genome annotation: application RT to a set of haloarchael genomes."; RL Life 5:1427-1444(2015). RN [4] {ECO:0000313|EMBL:DAC78034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78034.1}; RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.; RT "The genome of the Halobacterium salinarum type strain is closely RT related to that of the laboratory strains NRC-1 and R1."; RL Microbiol Resour Announc 0:0-0(2019). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000256|HAMAP-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|HAMAP- CC Rule:MF_01897}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP- CC 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 CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {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 EMBL; BK010829; DAC78034.1; -; Genomic_DNA. DR PIR; E84245; E84245. DR RefSeq; WP_010902625.1; NC_002607.1. DR PaxDb; Q9HR29; -. DR EnsemblBacteria; AAG19329; AAG19329; VNG_0889G. DR GeneID; 5953841; -. DR KEGG; hal:VNG_0889G; -. DR PATRIC; fig|64091.14.peg.683; -. DR eggNOG; arCOG04367; Archaea. DR eggNOG; COG0188; LUCA. DR InParanoid; Q9HR29; -. DR KO; K02469; -. DR OMA; THHWLLF; -. DR OrthoDB; 1547at2157; -. DR PhylomeDB; Q9HR29; -. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009330; C:DNA topoisomerase complex (ATP-hydrolyzing); IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central. DR GO; GO:0006261; P:DNA-dependent 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; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR InterPro; IPR013757; Topo_IIA_A_a_sf. 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|HAMAP-Rule:MF_01897}; KW Coiled coil {ECO:0000256|SAM:Coils}; 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 DOMAIN 19 470 TOP4c. {ECO:0000259|SMART:SM00434}. FT COILED 442 490 {ECO:0000256|SAM:Coils}. FT MOTIF 531 537 GyrA-box. {ECO:0000256|HAMAP-Rule: FT 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 //