ID Q9HR29_HALSA Unreviewed; 824 AA. AC Q9HR29; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 13-SEP-2023, entry version 133. 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; 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}, 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., Shukla H.D., RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R., RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J., RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., RA 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., Rodewald K., RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.; RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain RT 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 to a RT 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 related RT 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 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; 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 AlphaFoldDB; Q9HR29; -. DR STRING; 64091.VNG_0889G; -. DR PaxDb; Q9HR29; -. DR EnsemblBacteria; AAG19329; AAG19329; VNG_0889G. DR GeneID; 68693712; -. DR KEGG; hal:VNG_0889G; -. DR PATRIC; fig|64091.14.peg.683; -. DR HOGENOM; CLU_002977_6_1_2; -. DR OMA; THHWLLF; -. DR OrthoDB; 371943at2157; -. 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 type II (double strand cut, ATP-hydrolyzing) complex; 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 (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd00187; TOP4c; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1. DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1. DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 NCBIfam; TIGR01063; gyrA; 1. DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC/MITOCHONDRIAL; 1. DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000554}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897}. FT DOMAIN 19..470 FT /note="DNA topoisomerase type IIA" FT /evidence="ECO:0000259|SMART:SM00434" FT COILED 442..490 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 531..537 FT /note="GyrA-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897" FT ACT_SITE 130 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="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 //