GYRA_HELPY
ID GYRA_HELPY Reviewed; 827 AA.
AC P48370;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
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=HP_0701;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UC946;
RX PubMed=7695290; DOI=10.1128/aac.39.1.107;
RA Moore R.A., Beckthold B., Wong S., Kureishi A., Bryan L.E.;
RT "Nucleotide sequence of the gyrA gene and characterization of
RT ciprofloxacin-resistant mutants of Helicobacter pylori.";
RL Antimicrob. Agents Chemother. 39:107-111(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; L29481; AAA74376.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07753.1; -; Genomic_DNA.
DR PIR; E64607; E64607.
DR RefSeq; NP_207495.1; NC_000915.1.
DR RefSeq; WP_001153763.1; NC_018939.1.
DR AlphaFoldDB; P48370; -.
DR SMR; P48370; -.
DR DIP; DIP-3353N; -.
DR IntAct; P48370; 4.
DR MINT; P48370; -.
DR STRING; 85962.C694_03615; -.
DR PaxDb; P48370; -.
DR EnsemblBacteria; AAD07753; AAD07753; HP_0701.
DR KEGG; hpy:HP_0701; -.
DR PATRIC; fig|85962.47.peg.750; -.
DR eggNOG; COG0188; Bacteria.
DR OMA; THHWLLF; -.
DR PhylomeDB; P48370; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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..827
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145236"
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"
FT CONFLICT 4..5
FT /note="NS -> RL (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="M -> I (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> A (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="G -> E (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="H -> R (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="R -> Q (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Q -> P (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="N -> S (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="A -> V (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="D -> N (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="E -> G (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="E -> D (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="I -> M (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 686..687
FT /note="TT -> NA (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="K -> R (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="G -> E (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="T -> N (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 821..822
FT /note="SA -> PT (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="Missing (in Ref. 1; AAA74376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 827 AA; 92500 MW; 3631E6AFCF4279F2 CRC64;
MQDNSVNETK NIVEVGIDSS IEESYLAYSM SVIIGRALPD ARDGLKPVHR RILYAMHELG
LTSKVAYKKS ARIVGDVIGK YHPHGDNAVY DALVRMAQDF SMRLELVDGQ GNFGSIDGDN
AAAMRYTEAR MTKASEEILR DIDKDTIDFV PNYDDTLKEP DILPSRLPNL LVNGANGIAV
GMATSIPPHR MDEIIDALVH VLENPNAGLD EILEFVKGPD FPTGGIIYGK AGIIEAYKTG
RGRVKVRAKV HVEKTKNKEI IVLDEMPFQT NKAKLVEQIS DLAREKQIEG ISEVRDESDR
EGIRVVIELK RDAMSEIVLN HLYKLTTMET TFSIILLAIY NKEPKIFTLL ELLHLFLNHR
KTIIIRRTIF ELEKAKARAH ILEGYLIALD NIDEIVRLIK TSQSPEAAKN ALMERFTLSE
IQSKAILEMR LQRLTGLERD KIKEEYQNLL ELIDDLNGIL KSEDRLNGVV KTELLEVKEQ
FSSPRRTEIQ ESYENIDIED LIANEPMVVS MSYKGYVKRV DLKAYEKQNR GGKGKLSGST
YEDDFIENFF VANTHDILLF ITNKGQLYHL KVYKIPEASR IAMGKAIVNL ISLAPDEKIM
ATLSTKDFSD ERSLAFFTKN GVVKRTNLSE FESNRSCGIR AIVLDEGDEL VSAKVVDKNA
KHLLIASHLG IFIKFPLEEV REIGRTTRGV IGIKLNENDF VVGAVVISDD GNKLLSVSEN
GLGKQTLAEA YRGQSRGGKG VIGMKLTQKT GNLVGVISVD DENLDLMILT ASAKMIRVSI
KDIRETGRNA SGVKLINTAD KVMYVNSCPK EEEPENLETS SAQNLFE
