GYRA_BUCBP
ID GYRA_BUCBP Reviewed; 847 AA.
AC Q89AS3;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=bbp_169;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26902.1; -; Genomic_DNA.
DR RefSeq; WP_011091303.1; NC_004545.1.
DR AlphaFoldDB; Q89AS3; -.
DR SMR; Q89AS3; -.
DR STRING; 224915.bbp_169; -.
DR EnsemblBacteria; AAO26902; AAO26902; bbp_169.
DR GeneID; 56470712; -.
DR KEGG; bab:bbp_169; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000601; 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..847
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145225"
FT MOTIF 560..566
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 847 AA; 95830 MW; BCF78EEB59DD9939 CRC64;
MKEVAKEIIK IDIEDELKNS YLDYAMSVII GRALPDVRDG LKPVHRRILF AMKVLNNDWN
KTYKKSARIV GDVIGKYHPH GDTAVYDAIV RMAQPFSLRY VLIDGQGNFG SIDGDSAAAM
RYTEIRMSKI AYELLNDLDK NTVSFFSNYD GTEKIPEVLP AKIPNLLING SSGIAVGMAT
NIPPHNIKEV INGCLAFIDD QNITLKKLME HIPGPDFPTA GLINGKRGIE KAYKTGKGKI
YIRAKSIIEI QKKTKKKSII IYELPYQVNK ARVIKGIANL VKEKKIEGIT TLRDESDKEG
MRIVIEIKKE TKAEIILNQL YSLTQLEISF GINMVALIHG QPKVMTLKEI LNAFINHRRK
IIMRRSLFEL NKIRKKIHIL EGLIISLDNI DLIINLIKKS STLEEAKNKL KTYHWYSKHA
QYTQILKKNA HSLTPYDKKL RPIDTQKFFL TPEQIQAILE LRLQKLTHLE HKKLISEYKQ
LFKTSNNLEN ILKNNNILTK IMKDELIKIR DNFGDKRRTK INVNYSDINT SDLINKENVV
ITLSYSGYVK YQLLSSYEAQ KRGGKGKLAV KTKEEDFIEN LLVANTHDII LCFSSKGILY
WMKVYQLPEA SRHARGRPIV NLLPLSSNER ITAILPISEY KDSINIFMAT SKGMVKKTSL
YEFKKPRTKG IIAINLKADD ELIGVSLTNG NNTIMLFTAQ GKAVHFSEIL VRKTGRTAIG
VQGIKIKKSD KVVSLVVPKK HGNILLITEH GYGKRTEIHE FPIKSRATQG TIAMKITKKN
GIVIGTMQVV NQDQIIIITN AGTLVRTRVL EIGILGRNTQ GVIIIRTSKK EKVVALQKAN
ALHLNSV
