GYRA_CHLPN
ID GYRA_CHLPN Reviewed; 834 AA.
AC Q9Z8R4; Q9JRY7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
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};
GN OrderedLocusNames=CPn_0274, CP_0485, CpB0281;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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; AE001363; AAD18423.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38315.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98484.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98214.1; -; Genomic_DNA.
DR PIR; B86525; B86525.
DR PIR; F81571; F81571.
DR PIR; G72098; G72098.
DR RefSeq; NP_224479.1; NC_000922.1.
DR RefSeq; WP_010892079.1; NZ_LN847221.1.
DR AlphaFoldDB; Q9Z8R4; -.
DR SMR; Q9Z8R4; -.
DR STRING; 115711.CP_0485; -.
DR EnsemblBacteria; AAD18423; AAD18423; CPn_0274.
DR EnsemblBacteria; AAF38315; AAF38315; CP_0485.
DR GeneID; 45050323; -.
DR KEGG; cpa:CP_0485; -.
DR KEGG; cpj:gyrA_1; -.
DR KEGG; cpn:CPn_0274; -.
DR KEGG; cpt:CpB0281; -.
DR PATRIC; fig|115713.3.peg.307; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..834
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145229"
FT REGION 810..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 232
FT /note="T -> A (in Ref. 1; AAD18423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 93839 MW; A2C43C31A6C7B19C CRC64;
MFNKDEIIVP KNLEEEMKES YLRYSMSVII SRALPDIRDG LKPSQRRVLY AMKQLSLSPG
AKHRKCAKIC GDTSGDYHPH GESVIYPTLV RMAQNWAMRY PLVDGQGNFG SIDGDPPAAM
RYTEARLTHS AMYLMEDLDK DTVDIVPNYD ETKHEPVVFP SKFPNLLCNG SSGIAVGMAT
NIPPHNLGEL IEATLLLLAN PQASVDEILQ VMPGPDFPTG GIICGSEGIR STYTTGRGKI
KVRARLHVEE NEDKHRESII ITEMPYNVNK SRLIEQIANL VNEKTLAGIS DVRDESDKDG
IRVVLEIKKG ESSEIIINRL YKFTDVQVTF GANMLALDKN LPRTMSIHRM ISAWIRHRKE
VIRRRTRYEL NKAETRAHVL EGYLKALSCL DALVKTIRES GNKEHAKERI IESFGFTEPQ
ALAILELRLY QLTGLEAEKI QKEYEELLNK IAYYKQVLSD EGLVKDIIRN ELQDLLKHHK
VARRTTIEFD ADDIRDIEDI ITNESVIITI SGDDYVKRMP VKVFKEQRRG GHGVTGFDMK
KGAGFLKAVY SAFTKDYLLI FTNFGQCYWL KVWQLPEGER RAKGKPIINF LEGIRPGEEL
AAILNIKNFD NAGFLFLATK RGVVKKVSLD AFSNPRKKGI RALEIDEGDE LIAACHIVSD
EEKVMLFTHL GMAVRFPHEK VRPMGRTARG VRGVSLKNEE DKVVSCQIVT ENQSVLIVCD
QGFGKRSLVE DFRETNRGGV GVRSILINER NGNVLGAIPV TDHDSILLMS SQGQAIRINM
QDVRVMGRST QGVRLVHLKE GDALVSMEKL SSNENDDEVL SGSEEECSDT VSLR
