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 03-AUG-2022, entry version 122.
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}.
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DR EMBL; BA000003; BAB12897.1; -; Genomic_DNA.
DR RefSeq; NP_240011.1; NC_002528.1.
DR RefSeq; WP_010895986.1; NC_002528.1.
DR AlphaFoldDB; P57277; -.
DR SMR; P57277; -.
DR STRING; 107806.10038862; -.
DR PRIDE; P57277; -.
DR EnsemblBacteria; BAB12897; BAB12897; BAB12897.
DR KEGG; buc:BU180; -.
DR PATRIC; fig|107806.10.peg.191; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
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: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_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
