GYRA_ALKHC
ID GYRA_ALKHC Reviewed; 833 AA.
AC O50628; Q9JPZ0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=BH0007;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RA Masui N., Nakasone K., Horikoshi K.;
RT "Cloning and expression of the genes encoding DNA gyrase from alkaliphilic
RT Bacillus sp. strain C-125.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10427704; DOI=10.1271/bbb.63.1134;
RA Takami H., Masui N., Nakasone K., Horikoshi K.;
RT "Replication origin region of the chromosome of alkaliphilic Bacillus
RT halodurans C-125.";
RL Biosci. Biotechnol. Biochem. 63:1134-1137(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; AB010081; BAA24188.1; -; Genomic_DNA.
DR EMBL; AB013492; BAA82691.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB03726.1; -; Genomic_DNA.
DR PIR; G83650; G83650.
DR PIR; T46552; T46552.
DR RefSeq; WP_010896191.1; NC_002570.2.
DR AlphaFoldDB; O50628; -.
DR SMR; O50628; -.
DR STRING; 272558.10172619; -.
DR EnsemblBacteria; BAB03726; BAB03726; BAB03726.
DR KEGG; bha:BH0007; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000001258; 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..833
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145220"
FT REGION 803..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 525..531
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 806..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 833 AA; 93873 MW; 176EBB398C7F136B CRC64;
MAEQDQSRVK EINISQEMKT SFMDYAMSVI VSRALPDVRD GMKPVHRRIL YAMNELGMTS
DKAYKKSARI VGEVIGKYHP HGDSAVYETM VRMAQDFSYR YMLVDGHGNF GSIDGDAAAA
MRYTEARMSK ISMELVRDIN KDTIDYQDNY DGSEKEPVVM PSRFPNLLVN GASGIAVGMA
TNIPPHQLGE VIDGVLALSK NPDISVPELM EHIPGPDFPT GAEILGRSGI RKAYQTGRGS
ITLRAKTEIE EHHGKQRIIV HEIPYQVNKA KLIEKIAELV RDKKIDGITD LRDESDRNGM
RIVIEVRKDA NANVLLNNLY KQTALQTSFG INLLALVEGQ PKVLNLKECL EHYLAHQVIV
IRRRTAFELR KAEARAHILE GLRIALDHLD EVISLIRSSQ TTEIARNGLM ERFELSYEQA
QAILDMRLQR LTGLERDKIE AEYKELIERI AELKAILADH EKVLDIIREE LLELKEKYND
ERKTAISASE DMFEDEDLIP RQNVVITLTH HGYIKRLPIS TYRSQKRGGR GIQGMGTNED
DFVQHLFTTN SHHTILFFTN KGKVYRLKGY EIPELGRTAK GIPIINLLQI EQDEYISTII
PIEEFTEDHY LFFMTKDGIA KRTQLSSFAN IRRGGLFAIN LREGDELHGV RLTNGDKEVI
VGTRQGMAIR FHETDVRLMG RTATGVKGIS LTGDDHVVGM DIVEDGQDVL IVTEKGFGKR
TPIADYRIQT RGGKGIKTCN ITEKNGPLVS LKVVSVDHDL MIITASGIII RLHVKDISVT
GRITQGVTLI RVAEGEEVAT VARVDIEDDE LDEDESIEEE RDDRSEVEQG ENE
