ID   GYRA_CHLTR              Reviewed;         836 AA.
AC   O84192;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=CT_189;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
RC   STRAIN=L2;
RA   Dessus-Babus S., Bebear C.M., Charron A., Bebear C., de Barbeyrac B.;
RT   "Sequencing of gyrase and topoisomerase IV QRDRs of Chlamydia trachomatis
RT   and characterization of quinolone-resistant mutants obtained in vitro.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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; AE001273; AAC67781.1; -; Genomic_DNA.
DR   EMBL; AF044267; AAC33552.1; -; Genomic_DNA.
DR   PIR; F71546; F71546.
DR   RefSeq; NP_219693.1; NC_000117.1.
DR   RefSeq; WP_009871535.1; NC_000117.1.
DR   AlphaFoldDB; O84192; -.
DR   SMR; O84192; -.
DR   STRING; 813.O172_01020; -.
DR   PRIDE; O84192; -.
DR   EnsemblBacteria; AAC67781; AAC67781; CT_189.
DR   GeneID; 884941; -.
DR   KEGG; ctr:CT_189; -.
DR   PATRIC; fig|272561.5.peg.203; -.
DR   HOGENOM; CLU_002977_6_1_0; -.
DR   InParanoid; O84192; -.
DR   OMA; THHWLLF; -.
DR   Proteomes; UP000000431; 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..836
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145230"
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   836 AA;  94233 MW;  AA750FA55138B5FC CRC64;
     MLNKEEIIVP KNLEEEMKES YLRYSMSVII SRALPDARDG LKPSQRRILY AMKQLNLTPG
     VKHRKCAKIC GDTSGDYHPH GESVIYPTLV RMAQDWAMRY PLVDGQGNFG SIDGDPAAAM
     RYTEARLTHS AIFLLEDLDK DTVDMVPNYD ETKYEPVVFP SKFPNLLCNG SSGIAVGMAT
     NIPPHNLGEL IEATLLVLAN SQTSIEDILE VMPGPDFPTG GIICGTEGIR STYYTGRGKL
     RLRARMHVEE NSDKQRENII LTEMPYNVNK SRLIEQIAEL INEKTLTGIS DVRDESDKDG
     IRVVLELKKG ESSEVVINRL YKFTDVQVTF GANMLALDKN LPRTMNIHRM ISAWIRHRMD
     VIQRRTRYEL NKAEARAHIL EGFLKALSCM DEVVKTIRES SNKEHAKQQL VELFSFSEAQ
     ALAILELRLY QLTGLEADKV QKEYSELLEK ITYYRKVLAE EELVKDIIRE ELQELHKVHK
     TPRRTRIEMD AGDVRDIEDI ISDESVIITI SGDDYVKRMP VKVFREQKRG GQGVTGFDMK
     KGSDFLKAVY SASTKDYLLI FTNFGQCYWL KVWRLPEGER RAKGKPIINF LEGIRPGEQV
     AAVLNVKRFE QGEYLFLATK KGVVKKVSLD AFGSPRKKGI RALEIDDGDE LIAARHIAND
     EEKVMLFTRL GMAVRFPHDK VRPMGRAARG VRGVSLKNEQ DFVVSCQVVT EDQSVLVVCD
     NGFGKRSLVC DFRETNRGSV GVRSIVINQR NGDVLGAISV TDCDSILLMS AQGQAIRINM
     QDVRVMGRAT QGVRLVNLRE GDTLVAMEKL SINTESVETE ENLAASVQSG QDTIEE