GYRA_KOSOT
ID GYRA_KOSOT Reviewed; 812 AA.
AC C5CHA8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Kole_0018;
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga.
OX NCBI_TaxID=521045;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) 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; CP001634; ACR78747.1; -; Genomic_DNA.
DR RefSeq; WP_012744535.1; NC_012785.1.
DR AlphaFoldDB; C5CHA8; -.
DR SMR; C5CHA8; -.
DR STRING; 521045.Kole_0018; -.
DR EnsemblBacteria; ACR78747; ACR78747; Kole_0018.
DR KEGG; kol:Kole_0018; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000002382; 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..812
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409826"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 812 AA; 90484 MW; DA9C8469C7B2B86B CRC64;
MPEEIISRSI NDEMITSYML YSMSVIVGRA IPDVRDGLKP VQRKILFGML ELGLRHNQSY
KKSARIVGEV MGKFHPHGDM AIYDALVRMA QPFSMRYPLI QGQGNFGSID RDPPAAMRYT
EARMQRLAEE LLADIDKNTV KMIPNFDGSL IEPEVLPAKA PNLLMNGASG IAVGMMTNIP
PHNLSELVEA LTALIDNPDA TIEELMEYVK GPDFPTGGII MGRDGIKKMY ETGRGRMVVR
GVAEIEEAKG GTRIVISEIP YGVSKADLIQ QIANVAQNVR DIQVRNVRDE SDKRGLRVVI
ELKRGADPNV VLNLLYKHTQ LQTTFGAHML VIDEKKRPKL MNLKEIFQAF IKHRYEVVKR
RTEYELEQAS KKAHILEGLT KASRAIDTVV DIIRNSKNIQ EASVNLQETL EITPEQSQAI
LEMRLGKLTA LEIDKLVTEY AELVEKIKEY REILSDDKNI YQIIKKELQE LEAQYGDARR
TKISIDGNTD FNVEDVIPDD EVVVTVTKKG YIKATPLEDY RKQGRGGKGI RGVKTTDADF
VTNVVSTTRL SKTVVITSKG KAYFINNYEL ECTSRSSRGK LLANYVKIEP DETVQAVLSV
KREEVANKHL IITTRKGKIK RTPFEAFINS RTSGIKAITL NEGDSVVDAG ISTSEEETII
ISTRKGMVIR FPISQIRPMG RTAAGVKAMA LRGDDEVVSA TIVLPVDERY LFTATERGVG
KRTPLSEYRP QHRAGMGVKN IYGLERTGYV VGSLVVTNED EIIVITKNGM SIRIPAADIR
PTGRVTKGVK VVELRDDDTV ASLAVVVDQA EV
