GYRA_PSEAE
ID GYRA_PSEAE Reviewed; 923 AA.
AC P48372;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=PA3168;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7811002; DOI=10.1128/aac.38.9.1944;
RA Kureishi A., Diver J.M., Beckthold B., Schollaardt T., Bryan L.E.;
RT "Cloning and nucleotide sequence of Pseudomonas aeruginosa DNA gyrase gyrA
RT gene from strain PAO1 and quinolone-resistant clinical isolates.";
RL Antimicrob. Agents Chemother. 38:1944-1952(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; L29417; AAA68625.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06556.1; -; Genomic_DNA.
DR PIR; H83248; H83248.
DR RefSeq; NP_251858.1; NC_002516.2.
DR RefSeq; WP_003091448.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; P48372; -.
DR SMR; P48372; -.
DR STRING; 287.DR97_4768; -.
DR ChEMBL; CHEMBL3390828; -.
DR PaxDb; P48372; -.
DR PRIDE; P48372; -.
DR EnsemblBacteria; AAG06556; AAG06556; PA3168.
DR GeneID; 882800; -.
DR KEGG; pae:PA3168; -.
DR PATRIC; fig|208964.12.peg.3311; -.
DR PseudoCAP; PA3168; -.
DR HOGENOM; CLU_002977_6_1_6; -.
DR InParanoid; P48372; -.
DR OMA; THHWLLF; -.
DR PhylomeDB; P48372; -.
DR BioCyc; PAER208964:G1FZ6-3228-MON; -.
DR Proteomes; UP000002438; 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..923
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145245"
FT REGION 881..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 561..567
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 890..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 923 AA; 101135 MW; 0025DFE08CDD1BEC CRC64;
MGELAKEILP VNIEDELKQS YLDYAMSVIV GRALPDARDG LKPVHRRVLY AMSELGNDWN
KPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDNAAAM
RYTEVRMAKL AHELLADLEK ETVDWVPNYD GTEQIPAVMP TKIPNLLVNG SSGIAVGMAT
NIPPHNLGEV IDGCLALMDN PDLTVDELMQ YIPGPDFPTA GIINGRAGII EAYRTGRGRI
YIRARAVVEE MEKGGGREQI IITELPYQLN KARLIEKIAE LVKEKKIEGI SELRDESDKD
GMRVVIELRR GEVGEVVLNN LYAQTQLQSV FGINVVALVD GQPRTLNLKD MLEVFVRHRR
EVVTRRTVYE LRKARERGHI LEGQAVALSN IDPVIELIKS SPTPAEAKER LIATAWESSA
VEAMVERAGA DACRPEDLDP QYGLRDGKYY LSPEQAQAIL ELRLHRLTGL EHEKLLSEYQ
EILNLIGELI RILTNPARLM EVIREELEAV KAEFGDARRT EIVASQVDLT IADLITEEDR
VVTISHGGYA KSQPLAAYQA QRRGGKGKSA TGMKDEDYIE HLLVANSHAT LLLFSSKGKV
YWLRTFEIPE ASRTARGRPL VNLLPLDEGE RITAMLQIDL EALQQNGGAD DDLDEAEGAV
LEGEVVEAAE VEEVEGETAE LVAEPTGAYI FMATAFGTVK KTPLVQFSRP RSSGLIALKL
EEGDTLIAAA ITDGAKEVML FSSAGKVIRF AESVVRIMGR NARGVRGMRL GKGQQLISML
IPESGAQILT ASERGFGKRT PLSKFPRRGR GGQGVIAMVT NERNGALIAA VQVQEGEEIM
LISDQGTLVR TRVDEVSLSG RNTQGVTLIK LASDEVLVGL ERVQEPSGGD DEDLPEGEEA
AESLGESAES ESEPAAEAEG NEE
