ID A0A0F9YC15_9BACT Unreviewed; 908 AA.
AC A0A0F9YC15;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=UR12_C0015G0009 {ECO:0000313|EMBL:KKP29119.1};
OS candidate division TM6 bacterium GW2011_GWF2_30_66.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619078 {ECO:0000313|EMBL:KKP29119.1, ECO:0000313|Proteomes:UP000034862};
RN [1] {ECO:0000313|EMBL:KKP29119.1, ECO:0000313|Proteomes:UP000034862}
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:KKP29119.1}.
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; LBOA01000015; KKP29119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YC15; -.
DR STRING; 1619078.UR12_C0015G0009; -.
DR PATRIC; fig|1619078.3.peg.494; -.
DR Proteomes; UP000034862; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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}; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 23..475
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 887..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..495
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 536..542
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 134
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 908 AA; 100716 MW; ABBC23E5B68C9FB0 CRC64;
MEPLDNKGEL PGLNGTNPGI KPVLIETELK ESFLDYAMSV IVSRAIPDVR DGLKPVHRRV
LYTMHKLGFY HNKPYHKSVR VVGEVLGKYH PHGDQAVYGT MVGMVQDFSK RYPLLDGQGN
WGSVDGDNAA AMRYTEVRMM KVSQEILADL EKETVDFVPN FDESTVEPVI LPSRLPNLLV
NGTAGIAVGM ATSIPPHNLG EVINACLRLL EKPEASDEEI FDLIPAPDFP TGGVICGRSG
IIKGYKTGRG RVVVRGVVET EETKKGSRLI VTELPYQVNK AELIIKIADL VKNKIIDGIS
NIRDESDKQG MRVVIEIKKG EIPEVVLNQL YKHTPLQSAF SILMLALLDN KPLVFTLKQL
LQHFIEHRKQ VVYKRTVYDL TKAQEREHIL AGFIIALQNI DEVIVLIKKS KNADEAIIEL
NRRYLLTAKQ GKAILEMRLQ RLTGMEQDKI YADLEEIKKE IAFLRAILED QEVLKKEVVA
ELEEVKKNYS DARRSKISGP VDVLTEADLI PDEDVVVTIT CKGYIKRVDL STYDVQHRGG
KGKMGMASLE EKDDFVQDLF VAKNHDSLLF FTNLGRVYGM SVFEVPEGSR TSKGRAVVNI
LPLAQDEKVV KLLCTRGMEG KFIMMITKDG IVKRTDAESF SKIRVSGIRG ITLREGDELA
FCNMSSGNGS VVIATAKGQG IRFSEEEVRV MGRQASGVIG IRCREGDYVV GMEIIPGQDG
EILFATENGY GKQVTVEDFR LAHRGGVGVR TIPTDKRNGL VIGLAIIYED SNILLIDGGG
KIIRLSPKEI RTMGRQAKGV RLIRLEEGQK LATVVAFRED DKVEGQDDPE AGGEVDPKKE
IQAKIKAAAR EIKQASLNGD SQDLESIDSV NLDGEFALED QAVDGFDASE DDQILDSSSQ
DQDIFNQF
//
