ID   GYRA_UREPA              Reviewed;         840 AA.
AC   Q9PR63;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   10-JUN-2026, entry version 131.
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=UU082;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(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; AF222894; AAF30487.1; -; Genomic_DNA.
DR   RefSeq; WP_006688806.1; NC_002162.1.
DR   AlphaFoldDB; Q9PR63; -.
DR   SMR; Q9PR63; -.
DR   STRING; 273119.UU082; -.
DR   EnsemblBacteria; AAF30487; AAF30487; UU082.
DR   GeneID; 29672273; -.
DR   KEGG; uur:UU082; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_14; -.
DR   OrthoDB; 9806486at2; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:TreeGrafter.
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:UniProtKB-ARBA.
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   FunFam; 1.10.268.10:FF:000001; DNA gyrase subunit A; 1.
DR   FunFam; 3.30.1360.40:FF:000002; DNA gyrase subunit A; 1.
DR   FunFam; 3.90.199.10:FF:000001; DNA gyrase subunit A; 1.
DR   FunFam; 2.120.10.90:FF:000005; DNA topoisomerase 4 subunit A; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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   InterPro; IPR050220; Type_II_DNA_Topoisomerases.
DR   NCBIfam; TIGR01063; gyrA; 1.
DR   NCBIfam; NF004043; PRK05560.1; 1.
DR   NCBIfam; NF004044; PRK05561.1; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS52040; TOPO_IIA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
FT   CHAIN           1..840
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145272"
FT   DOMAIN          51..516
FT                   /note="Topo IIA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT   MOTIF           543..549
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        139
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   840 AA;  94252 MW;  8D3DC66EB4DC1CF3 CRC64;
     MALKKPKKSR LTTEEIKQQL EGSTIKEQSI TKEVETSFLD YSMSVIVARA LPDVRDGFKP
     VHRRALFAAF ENGMTHDKPY KKSARWVGDV IGKYHPHGDQ AVYQTIVRMA QDFSMRYLLV
     DGHGNFGSID GDSAAAMRYT EARLSKISYE LLKYIDKETV DFVPNYDASE QEPSVLPSGF
     PNLLTNGTTG IAVGMATNIP PHNLTEVCQA IKAYAKNHNV TISEIMEYLK GPDFPTGAEI
     YGDSGIIKYF NTGRGSVTIR SKYEIEDIGQ GRVAIVVTEI PYMVNKANLI EKIVELVTNK
     QIEGISDLRD ESSRDGIRIV IEVKRDVIPE VLLNKLFKTT PLQTNFSVNN LALVNGVPMV
     LNIKEMIKYY FEHQIEILVR RTNFDLKKAK ERIHIVEGLV IAVNNIDEVI KIIKASGDDD
     IASKSLIQRF DLTELQTKAI LEMRLRALTG LNIDKLKKEY EDLILVIKDL EDVLNNYNRQ
     VNIICENLDY LIEKFGDERR TEIMYGVSSH IDDEDLIPVE DIVVTMSKRG YFKRLPIDTY
     KNQRRGGVGV QGLKTYEDDD VEKILVANTH TDLLFFSDLG RVYRLRGHEV PLGSRQSKGI
     PAINFLPIEK SESILTILPI DNYDQGSLFF TTSKGIIKRA NLSDFESIRA NGKIAITLKD
     GDKLFSVMQT LGNDEVFIGA SNGNVIRFNE NDAREMGRIA TGVKGINLEN DEYVVGTGLS
     SHGEYVLAVG SKGLGKLTDI NDYRLTKRGA KGVNTLKVND KTGNLVSIKV VNREEEALII
     TTSGKVIRLS IKDISVIGRN TSGVKLISLE NKEEVKSIAI FKKEEINDEQ LLQENDYNLK
//