GYRA_DEHLB
ID GYRA_DEHLB Reviewed; 814 AA.
AC D8K235;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=Dehly_1374;
OS Dehalogenimonas lykanthroporepellens (strain ATCC BAA-1523 / JCM 15061 /
OS BL-DC-9).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=552811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1523 / JCM 15061 / BL-DC-9;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Rainey F.A., Yan J.,
RA da Costa M.S., Moe W.M., Woyke T.;
RT "Complete sequence of Dehalogenimonas lykanthroporepellens BL-DC-9.";
RL Submitted (JUN-2010) 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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; CP002084; ADJ26663.1; -; Genomic_DNA.
DR RefSeq; WP_013218798.1; NC_014314.1.
DR AlphaFoldDB; D8K235; -.
DR SMR; D8K235; -.
DR STRING; 552811.Dehly_1374; -.
DR PRIDE; D8K235; -.
DR EnsemblBacteria; ADJ26663; ADJ26663; Dehly_1374.
DR KEGG; dly:Dehly_1374; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000002349; Chromosome.
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; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 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 Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..814
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409823"
FT MOTIF 526..532
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 814 AA; 90330 MW; CE87804D6287F8AD CRC64;
MVIGNTRPIN IEDEMKNSYM DYAMSVIVSR ALPDVRDGLK PVHRRILYAM SDLGMHYNTS
YKKSARIVGE VLGKYHPHGD SSVYDAMVRM AQNFSLRYML VDGQGNFGSV DGDPPAAMRY
TEARLTRLAG ELLVDIDKDT VEFMPNFDDS LKEPTVLPSR LPVLLMNGAS GIAVGMATNI
PPHNLTELCD AISYLIDNPE CGLEDLMQFV KGPDFPTGGL ILGRDGIKSA YATGHGKVVV
RARAHVADVA ETGARRQIII SELPYQVNKA DLVKRIAMLS RERKINGIAE VRDESDRQGL
RVVIELKRDG EPQQILNNLY KHTNLQTSFF VNMLALVNNR PVVLNLKEAL NHYVAFRQEI
ITRRSKFELK AARARAHILE GLKIALDNLD AIINLIRHAE NADTARRELM SRFELSQLQA
QAILDLQLRR LANLERQKIL GEYADILKQI SYLEDLLANP RKVLSLVKDD LAEVKARYGD
ARRTEIQSQG VIEFREEDLI PHQSMVVTLT ERGFIKRVPT EVYRLQHRAG RGKSIIKTRE
ADSVRFIMVA DTHDSVLLFT NRGKIFSIKC HEIPCDLLRT AKGIAIINLV PLAENERITS
MIAVSRFDEE TSLIMATSGG ECKRTKLSDF AAVRSSGLLA MDLPKNDELI GAVIAGADEN
IILITHNGRS IHFPVADLRV SQRASGGVRG ITLEGDDRVA GLDVARPGHF VLVVTTGGYG
KLTAVEEYPL QRRAGSGVLT FKVVDKTGKV AAGKVVDREH QVMIATAEGV VIRTPVGTED
QEKGIIVMGR STQGVIVIRP DENDRVVNFA TMVE
