ID A0A941RGT5_UNCPS Unreviewed; 919 AA. AC A0A941RGT5; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 29-MAY-2024, entry version 6. 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:MBS0185310.1}; GN ORFNames=JSS34_03020 {ECO:0000313|EMBL:MBS0185310.1}; OS Pseudomonadota bacterium. OC Bacteria; Pseudomonadota. OX NCBI_TaxID=1977087 {ECO:0000313|EMBL:MBS0185310.1, ECO:0000313|Proteomes:UP000749520}; RN [1] {ECO:0000313|EMBL:MBS0185310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS-1 {ECO:0000313|EMBL:MBS0185310.1}; RX PubMed=33819658; RA Wang Y., Zhao R., Liu L., Li B., Zhang T.; RT "Selective enrichment of comammox from activated sludge using RT antibiotics."; RL Water Res. 197:0-0(2021). RN [2] {ECO:0000313|EMBL:MBS0185310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS-1 {ECO:0000313|EMBL:MBS0185310.1}; RA Wang Y., Cao Y., Meng X., Hu T., Wang S., Cao K.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. 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 type II topoisomerase GyrA/ParC subunit CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP- CC Rule:MF_01897}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBS0185310.1}. 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; JAFEBT010000012; MBS0185310.1; -; Genomic_DNA. DR Proteomes; UP000749520; Unassembled WGS sequence. 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; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. 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}; 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}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_01897}. FT DOMAIN 14..492 FT /note="DNA topoisomerase type IIA" FT /evidence="ECO:0000259|SMART:SM00434" FT REGION 886..919 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 553..559 FT /note="GyrA-box" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897" FT COMPBIAS 904..919 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897" SQ SEQUENCE 919 AA; 103784 MW; E6174F2348099069 CRC64; MTDSIELHSD ISPVSLEDEM KRSYIDYAMS VIVSRALPDV RDGLKPVHRR ILFAMKEGGN EYNRPYRKSA RVVGDVIGKY HPHGEGAVYD SMVRMAQDFS MSAVLIDGQG NYGSMDGDPP AAMRYTETRL SQLAHFLLED LDKKTVNYRP NYDESLEEPV VLPARYPNLL VNGAGGIAVG MATNIPPHNL GEVIDACILQ IDNPFVTDEE MMEVIKGPDF PTGGQILGRH AVREAFLHGR GSVLMRAKTH IEEIRKDRMA IVATEIPYQV NKARLVERIA ETVTDKIIEG ISDLRDESDR DGVRVVIELK RDATPEVVLN QLFKHTPLQT SFGVNLLALH EGRPLLMGIR RVLECFIEFR EQVITNRTRF DLLKAQDRAH ILIGLAIAVA NIDPMIELIK KASDPQIARE KLMEIAWPAE TVASLLSLIQ EESHKVKDGK YLLSENQARA ILDLRLHRLT GLERDKIAQE LEEIIQQIKE FLAILASKPR RLEIMKTELL EIKEKFSVPR RTEIIDHIGD QDYEDLIERE DMVVTVSHAG YIKRVPLSTY RAQRRGGKGK TGMQTRDEDF VNQVFIANTH IPVFFFSSKG KVYQMKTYRL PLGSAQSRGK AMINLLPLEE GEIITTVLAL PEEKESWENL YILFATSLGN IRRNRLSDFS NIRSNGLIAI KLDDNEKLIG VHLCEENQDI LIATRLGKSI RFPLDALRVF AGRSSNGVRA IRLGKGDLVN SLSVINATQF TPEEREAYLR KANKDRRGEE IDFQEEDSEE ERTSSAFSIT EDLYRKMAEE EQFILTITEN GYAKRTSSYA YRRTNRGGQG VVNMTLGTKT GNVISSFPIE NEGQVILVTD QGQLIRCPVH DIRICGRQSQ GVILFRVGKD EKVASTAVVR EDNGEEELEE EIETSHPELI QDESSHDES //