ID   GYRA_CHLMU              Reviewed;         833 AA.
AC   Q9PKK4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-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=TC_0461;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(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; AE002160; AAF39312.1; -; Genomic_DNA.
DR   PIR; H81700; H81700.
DR   RefSeq; WP_010230505.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKK4; -.
DR   SMR; Q9PKK4; -.
DR   STRING; 243161.TC_0461; -.
DR   EnsemblBacteria; AAF39312; AAF39312; TC_0461.
DR   GeneID; 1245816; -.
DR   KEGG; cmu:TC_0461; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_0; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   Proteomes; UP000000800; 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   Topoisomerase.
FT   CHAIN           1..833
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145228"
FT   MOTIF           527..533
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   833 AA;  93884 MW;  D168FE5950D8D221 CRC64;
     MLNKEEIIVP KNLEEEMKES YLRYSMSVII SRALPDVRDG LKPSQRRILY AMKQLNLTPG
     AKHRKCAKIC GDTSGDYHPH GEAVIYPTLV RMAQDWAMRY PLVDGQGNFG SIDGDPAAAM
     RYTEARLTHS SIFLLEDLDK DTVDMVPNYD ETKYEPVVFP SKFPNLLCNG SSGIAVGMAT
     NIPPHNLGEL IEATLLVLAN PQTSIEEILE VMPGPDFPTG GIICGTEGIR STYYTGRGKL
     RLRARIHVEE NSDKQRENII LTEMPYNVNK SRLVEQIAEL INEKTLTGIS DVRDESDKDG
     IRVVLELKKG ESSEVIINRL YKFTDVQVTF GANMLALDKN LPRTMSIHRM ISAWIRHRMD
     VIRRRTRYEL NKAETRAHIL EGFLKALSCM DEVVKTIRES SNKEHAKQQL VELFGFSEAQ
     SLAILELRLY QLTGLEIDKV QKEYNELLEK IAYYRRVLAE EELVKDIIRE ELQELHKVHK
     TPRRTTIEMD AGDVRDIEDI IADESVIITI SGDDYVKRMP VKVFREQKRG GQGVTGFDMK
     KGSDFLKAVY SASTKDYLLI FTNMGQCYWL KVWQLPEGER RAKGKPIINF LEGIRPGEQV
     AAVLNVKRFE QGEYLLLATK KGVVKKVSLD AFGSPRKKGI RALEIDDGDE LIAARHIVND
     EEKVMLFTRL GMAVRFPHDK VRPMGRAARG VRGVSLKNEE DFVVSCQVVT DDQSVLVVCD
     NGFGKRSLVC DFRETNRGSV GVRSILINQR NGDVLGAISV TDFDSILLMS AQGQAIRINM
     QDVRVMGRAT QGVRLVNLRE GDTLVAMEKL SVNTESGETE ESVSIQVGHA VEE