ID A0A0G0RI21_9BACT Unreviewed; 945 AA.
AC A0A0G0RI21;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=UT42_C0048G0011 {ECO:0000313|EMBL:KKR13317.1};
OS Candidatus Falkowbacteria bacterium GW2011_GWA2_39_24.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1618634 {ECO:0000313|EMBL:KKR13317.1, ECO:0000313|Proteomes:UP000034048};
RN [1] {ECO:0000313|EMBL:KKR13317.1, ECO:0000313|Proteomes:UP000034048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR13317.1}.
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DR EMBL; LBWS01000048; KKR13317.1; -; Genomic_DNA.
DR PATRIC; fig|1618634.3.peg.532; -.
DR Proteomes; UP000034048; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..594
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 656..662
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 251
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 945 AA; 106922 MW; 1CFF47805C216FDC CRC64;
MTGRKKSEKT SNHQEIKQDE IDRLRAMLDH DEEAQIEKDM RELLHQRRQK IHRQVAEMES
RNKRLLMWSA IVVLMLIVIS FWLFKFNEIV SRPXXXXXXX XXXXXXXXXK IKKHKKTLKK
MDAVSTEPRT DNNLGNIEIQ PIVDEMRTSY LDYAMSVIVS RALPDVRDGL KPVHRRILYA
MWSIGLKANA KFRKSATVVG EVLGKYHPHG DSAVYDSMVR MAQDFAMRYP LVKGQGNFGS
MDADNPAAMR YTEAKLASIA EELLYDIDRK TVDFVPNFDG SQQEPKVLPS RLPNLLLNGS
MGIAVGMSTN IPPHNLRELS AAIQHLIDHP EAEVSDLMQF VQGPDFPTGG VIYNRQDIAQ
VYTTGKGGIV LRGVAEVVEK NGSNFQIIIS EIPYQVNKAA LVEKIADLVR EKKLEGIKDL
RDESNKDGVR IVIELKKDAY PKKILNALYK KTQLQETYHV NLLALVNGIQ PKVLNLKLAL
EEYIKHREEV VKRRTEFDLA KAKARAHILE GLMIALHNID AVIKVIKQSK DREMARINLQ
KQFKLTEIQA TAIVEMKLGN LANLERLRIE NELKEKKQLI KDLETILQSR TKILSIVKSE
LKELTEKYGD DRRTKVVVRG VKEFGVEDLV PNEEVVVMMT RDGYIKRLTR DTFKVQGRGG
KGVIGLTTKE EDGVEFMFST MTHDDILFFT SKGRVFQLKT HEIPAAQRTA KGQAIVNFLQ
LPTQERITSV LPLKKLNDYK FLFFATEKGL VKKVAIDAFN NVRRSGLIAI KLKEEDKLIW
IKPTTGKDTI QLITANGQAI HFKESDVRDM GRNAAGVLGI RLRKNDLVVG MGVVNGQKPM
KNYQVLGVMS KGFGKRTPLN LYKIQGRGGS GLKTAKVTPK TGPIANAYVV NFANMEDKDL
IIISAQGQVI RLPFKTVKKI GRDTQGIKLM SFKDKEDKIA GVTWL
//
