ID Q9HR29 PRELIMINARY; PRT; 824 AA. AC Q9HR29; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE DNA gyrase subunit A. GN Name=gyrA; OrderedLocusNames=VNG0889G; OS Halobacterium sp. (strain NRC-1 / ATCC 700922 / JCM 11081). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=64091; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=20504483; 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 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. CC -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA CC breakage and rejoining; the B chain catalyzes ATP hydrolysis. The CC enzyme forms an A2B2 tetramer (By similarity). 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; AE005028; AAG19329.1; -. DR PIR; E84245; E84245. DR HSSP; P09097; 1AB4. DR GO; GO:0005694; C:chromosome; IEA. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA. DR GO; GO:0006265; P:DNA topological change; IEA. DR GO; GO:0006268; P:DNA unwinding; IEA. DR InterPro; IPR005743; DNA_gyrA. DR InterPro; IPR006691; DNA_gyraseA_C. DR InterPro; IPR002205; DNA_topoisoIV. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR ProDom; PD000742; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. KW Complete proteome; DNA-binding; Isomerase; Topoisomerase. SQ SEQUENCE 824 AA; 90222 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 //