GYRA_HELPJ
ID GYRA_HELPJ Reviewed; 828 AA.
AC Q9ZLD9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=jhp_0641;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06219.1; -; Genomic_DNA.
DR PIR; E71906; E71906.
DR RefSeq; WP_001151036.1; NC_000921.1.
DR AlphaFoldDB; Q9ZLD9; -.
DR SMR; Q9ZLD9; -.
DR IntAct; Q9ZLD9; 1.
DR STRING; 85963.jhp_0641; -.
DR EnsemblBacteria; AAD06219; AAD06219; jhp_0641.
DR KEGG; hpj:jhp_0641; -.
DR eggNOG; COG0188; Bacteria.
DR OMA; THHWLLF; -.
DR Proteomes; UP000000804; 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 Topoisomerase.
FT CHAIN 1..828
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145237"
FT MOTIF 528..534
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 828 AA; 92651 MW; DE6E7DE4A7FBF150 CRC64;
MQDHLVNETK NIVEVGIDSS IEESYLAYSM SVIIGRALPD ARDGLKPVHR RILYAMHELG
LTSKVAYKKS ARIVGDVIGK YHPHGDTAVY DALVRMAQDF SMRLELVDGQ GNFGSIDGDN
AAAMRYTEAR MTKASEEILR DIDKDTIDFV PNYDDTLKEP DILPSRLPNL LVNGANGIAV
GMATSIPPHR IDEIIDALAH VLGNPNAELD KILEFVKGPD FPTGGIIYGK AGIVEAYKTG
RGRVKVRAKV HVEKTKNKEI IVLGEMPFQT NKAKLVEQIS DLAREKQIEG ISEVRDESDR
EGIRVVIELK RDAMSEIVLN HLYKLTTMET TFSIILLAIY NKEPKIFTLL ELLRLFLNHR
KTIIIRRTIF ELEKAKARAH ILEGYLIALD NIDEIVRLIK TSPSPEAAKN ALIERFSLSE
IQSKAILEMR LQRLTGLERD KIKEEYQNLL ELIDDLNGIL KSEDRLNEVV KTELLEVKEQ
FSSPRRTEIQ ESYESIDTED LIANEPMVVS MSYKGYVKRV DLKAYERQNR GGKGKLSGST
YEDDFIENFF VANTHDILLF ITNKGQLYHL KVYKIPEASR IAMGKAIVNL ISLAPNEKIM
ATLSTKDFSD ERSLAFFTKN GVVKRTNLSE FGGNRSYSGI RAIVLDEGDE LVGAKVVDKN
AKHLLIASYL GMFIKFPLED VREIGRTTRG VMGIRLNEND FVVGAVVISD DSNKLLSVSE
NGLGKQTLAE AYREQSRGGK GVIGMKLTQK TGNLVSVISV DDENLNLMIL TASAKMIRVS
IKDIRETGRN ASGVKLINTA DKVVYVNSCP KEEEPENLET SSVQNLFE
