ID G2LDP3_CHLTF Unreviewed; 816 AA.
AC G2LDP3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=Cabther_A2163 {ECO:0000313|EMBL:AEP12901.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP12901.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP12901.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP12901.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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; CP002514; AEP12901.1; -; Genomic_DNA.
DR RefSeq; WP_014100638.1; NC_016024.1.
DR AlphaFoldDB; G2LDP3; -.
DR STRING; 981222.Cabther_A2163; -.
DR KEGG; ctm:Cabther_A2163; -.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000006791; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000006791};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 9..466
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 438..465
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 816 AA; 90892 MW; 36EC0F3671F35258 CRC64;
MTEQKIIPAN IEDEMRRSYL DYAMSVIISR ALPDVRDGLK PVQRRVLWTM HELGNTYDKP
YKKSARVVGD AIGKYHPHGD QPVYDTIVRM AQDFSMRMPL IDGQGNFGSV DGDAAAAMRY
TEVRLAPIAE MLLADIEKET VDFQENYDNS LREPVVLPAR FPNVLVNGAA GIAVGMSTSI
PPHNLAEVLD ATIHLVNHPE ATVEELMQFI QGPDFPTAGF ICGRKGIRDA YLTGRGSVTM
RARAAIDYVA GKGERERQAI VVTELPYQVN KASLLEKIAE LVSEKKIEDI ADLRDESDRE
GMRIVIELKR GAVAQVVLNN LFKHTPMQEK FSIIMLAIVN RQPQILDLAE ILRHFIEHRR
EVVRRRTAFE LRKAEHRAHI LEGFKKALDV LDAVIALIRG AKSSAEAREG LMTRFALSQV
QAQSILEMQL QRLTGMERQK LLDEYENLLK RMAELREILE KETRLRAVIV QELQEVRKAY
STPRRTQIVD EGTDFTIEDL IPNEEVVITI TRGGYIKRTP LSAYRTQKRG GTGRRGMTTK
AEDVVEFLDI ASTHSFLLIF TAKGQVYKIK VHEIPDAATA GRGKAIVNLI ELPEGERVAG
TIAVREFTPG KFVVFVTRRG MIKKTELSEY ANIRSNGLIA MGVAEDDELI AVQKSDGNQH
ILISTFGGQA ICFNESDVRP MGRPAHGVIG IRLEENDYVT GMSVVGRTEE ILSVSELGLG
KRTPIMEYPV QHRGGKGVVT LNVTERTGGV VKVLPVQESK ELMVITQQGQ IVRVDVASIR
QTGRHAQGVK IITLAEDDRV VDASLVESSG EETGAD
//
