(data stored in SCRATCH3701 zone)

SWISSPROT: GYRA_BUCAI

ID   GYRA_BUCAI              Reviewed;         830 AA.
AC   P57277;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   11-DEC-2019, entry version 116.
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=BU180;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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}.
DR   EMBL; BA000003; BAB12897.1; -; Genomic_DNA.
DR   RefSeq; NP_240011.1; NC_002528.1.
DR   RefSeq; WP_010895986.1; NC_002528.1.
DR   SMR; P57277; -.
DR   STRING; 107806.10038862; -.
DR   PRIDE; P57277; -.
DR   EnsemblBacteria; BAB12897; BAB12897; BAB12897.
DR   GeneID; 1109623; -.
DR   KEGG; buc:BU180; -.
DR   PATRIC; fig|107806.10.peg.191; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   Proteomes; UP000001806; 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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
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;
DR   PRODOM; P57277.
DR   SWISS-2DPAGE; P57277.
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_0000145223"
FT   MOTIF           541..547
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   830 AA;  93879 MW;  29B995C7B09A9073 CRC64;
     MKDPSREIIQ VNIEEELKSS YLDYSMSVIV GRALPDVRDG LKPVHRRILF AMYILNNDWN
     KAYKKSARIV GDVIGKYHPH GDSAVYDAIV RMAQKFSLRY MLIDGQGNFG SVDGDSAAAM
     RYTEVRMSKI AHELLNDLEK NTVEFLPNYD GTEYIPEILP AKIPNLLING SSGIAVGMAT
     NIPPHNLNEV INGCLAYIDN NDITLEELIK HIPGPDFPTA AIINGKSGIE EAYRTGKGKI
     YIRAQNQIEK NKKNKKESIV FNEIPYQVNK SRLIEKIAEL VKEKRIDGIT ALRDESDKDG
     MRIVIEIKRE AIAEVILNQL YSLTQLQISF GINMVALCQG QPKTLSLKEI LKNFLSHRQE
     IIIRRSLFEL NKVRNRIHIL EGLNMALINI NAIIEIIKNS VNSIDAKKII IQKNWKSEKI
     NYLAKKHEYY FSEKQAQAIL DLRLHKITNL EQEKIIMEHN DLIKKTKELK EILENPKKMF
     EVIKSELLSI QNNFSDKRRT KITENHSDIN MEDLINQEDV VVTLSHSGYV KYQPLSDYNA
     QRRGGKGKSA AKIKEEDFIE SLVIANTHDT ILCFSSRGIL YWMKVYQLPE SSRHARGRPI
     VNLLPLSPKE RITAILPVHK YQDNLNIFMT TAHGIVKKSS LSQFKKPRFA GIIAINLHAN
     DELIGVALTD GNNNIMLFTQ NGKVVQFLEN SVRTMGRTAS GVKGIKIKKN DKVVSLIVPK
     NKGSILIATK NGYGKRTKIS DFPIKSRATQ GVISIKITKK NGKIIGAIQV IEKDQIMMIT
     DAGTLVRIRV SEVGVLKRNT QGVILIRTSK NEKVVALQKI VDPMIEKIDL
//

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