GYRA_CLOAB
ID GYRA_CLOAB Reviewed; 830 AA.
AC P94605;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=CA_C0007;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RA Ullmann S., Duerre P.;
RT "Nucleotide sequence and molecular characterization of the DNA gyrase genes
RT from Clostridium acetobutylicum.";
RL Anaerobe 2:239-248(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; U35453; AAB41131.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK77994.1; -; Genomic_DNA.
DR PIR; G96900; G96900.
DR PIR; T46556; T46556.
DR RefSeq; NP_346654.1; NC_003030.1.
DR RefSeq; WP_010963336.1; NC_003030.1.
DR AlphaFoldDB; P94605; -.
DR SMR; P94605; -.
DR STRING; 272562.CA_C0007; -.
DR EnsemblBacteria; AAK77994; AAK77994; CA_C0007.
DR GeneID; 44996480; -.
DR KEGG; cac:CA_C0007; -.
DR PATRIC; fig|272562.8.peg.186; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000814; 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..830
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145231"
FT REGION 805..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 524..530
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 810..830
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT CONFLICT 766..768
FT /note="GIA -> HS (in Ref. 1; AAB41131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 92612 MW; 1508C0CB16E82252 CRC64;
MLNEGKVLPV DISSEMKKCY IDYAMSVIVS RALPDVRDGL KPVHRRILYS MHELGLTPEK
GYRKCARIVG DVLGKYHPHG DSSVYGALVR LAQDFNLRYT VVDGHGNFGS VDGDSAAAMR
YTEAKMNKIA LEMVRDIGKN TVDFIPNFDG EEKEPVVLPS RFPNLLVNGS AGIAVGMATN
IPPHNLGEVI DGITMLIDNP EATILELMAQ IKGPDFPTAG IIMGKSGIRA AYETGRGKIT
VRAKSEIEVE DNGKQKIIIT EIPYQVNKAR LVESIADLVK DKRIVGISDL RDESDRDGMR
IVIEIKKDAN SNIILNQLYK HTRLQDTFGI NMLALVDNRP EVLNLKQILQ HYIKFQEQVI
RRRTEFDLEK ASARAHILEG LKIALDHIDE VISLIRGSKT AQEAKLGLMD KFGLSEKQAQ
AILDLKLQRL TGLEREKIED EYNELMKTIA ELKSILADEN KILAIIRDEL NEIKAKYGDE
RKTAIERAEN DIDIEDLIQE ENVVITLTHA GYIKRINADT YTSQKRGGRG IQAMTTKEDD
FVENIFITST HNNILFFTNK GRMYKLKAYQ IPEAGRAAKG TNVVNLLQLD PNEKIQAVIS
IKEFDEESFL VMCTKKGIIK KTVVGMYKNI RKSGLIAINL NDDDELVSVR ITKGDDDIII
VTNKGLAIRF NEVDVRPLGR NALGVKGITL KEDDFVVGME VPNQESDVLV VSENGFGKRT
HVGEYKCQHR GGKGLITYKV SDKTGKLVGV RMVEDGDELM LINNLGIAIR INVSDISTTS
RNAMGVTLMR NNGDEKVLAL AKINKDDSEQ LEDSEEVSEV HDAEENNSEE
