ID   E3EDT0_PAEPS            Unreviewed;       854 AA.
AC   E3EDT0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   01-MAY-2013, entry version 21.
DE   RecName: Full=DNA gyrase subunit A;
DE            EC=5.99.1.3;
GN   Name=gyrA; OrderedLocusNames=PPSC2_c0008;
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=886882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2;
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J.,
RA   Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of
RT   plant growth-promoting Rhizobacterium with broad-spectrum
RT   antimicrobial activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       Within the heterotetramer, GyrA contains the active site tyrosine
CC       that forms a covalent intermediate with the DNA, while GyrB
CC       contributes the cofactor binding sites and catalyzes ATP
CC       hydrolysis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
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DR   EMBL; CP002213; ADO53996.1; -; Genomic_DNA.
DR   RefSeq; YP_003944237.1; NC_014622.1.
DR   EnsemblBacteria; ADO53996; ADO53996; PPSC2_c0008.
DR   GeneID; 9848335; -.
DR   KEGG; ppm:PPSC2_c0008; -.
DR   PATRIC; 42503290; VBIPaePol172748_0009.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; IAQEDVV; -.
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:HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 2.
DR   HAMAP; MF_01897; GyrA; 1; -.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013760; Topo_IIA_like_dom.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; gyrA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
FT   ACT_SITE    123    123       O-(5'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
SQ   SEQUENCE   854 AA;  95760 MW;  C928C8ECA111C3EB CRC64;
     MADQNNSQII NRDIGVEMRE SFMDYAMSII VSRALPDVRD GLKPVHRRIL YAMSELGMSP
     DKPYKKSARI VGEVIGKYHP HGDTAVYDTM VRMAQDFSLR YMLVDGHGNF GSVDGDMAAA
     MRYTEARLSK IAMEMLRDLN KETVDFMPNY DGEENEPVVL PARYPNLLVN GVGGIAVGMA
     TNIPPHNLGE VIDGVQALIE NPDITPMELM DYIQGPDFPT AGYILGRSGI RQAYQTGRGS
     VTMRAKTTIE EIGNKARIIV HELPYQVNKA RLVEKIAELV RDKRIEGITD LRDESDRTGM
     RIVIELRRDV NPNVVLNNLF KHTAMQSNFG INMLAIVNNE PKILNLKDVL YYYLKHQIEV
     IRRRTEFDLK KAEARAHILE GLRIALDHLD EVISLIRSSQ TAEAAREGLI ERFSLTLEQA
     QAILDMRLQR LTGLEREKIE NEYNELIQKI MEYREILANE HLVLNIISEE LNELKGRFAD
     DRRTEITVGE ESILDEDLIP REDVIITVTH TGYIKRLPVT TYRSQKRGGR GVVGMDTKDE
     DFVEHLFITN SHHHLLFFTD KGKVYRIKAY EIPDLSRTAR GTPIINLIQI EQGESINAVI
     PIEEFVEDSY LFFATQHGII KKTPLDDYAN IRKGGLIAIN LREDDALIEV KLTDGQQEMI
     IGTAQGMSIR FPESDVRSMG RSATGVKGIS LDESDAVIGM DIVNTDLDIL IVTAKGYGKR
     TPAVDYRIQS RGGKGIKTIN VTDKNGPVVG LKVVKAEEDL MIITASGTLI RTSMGEISTM
     GRNTQGVRLI NIRDDDSVAT VCRANKNEEQ DELLEDLLED GGTGEEPTLS SAEPTLEVNT
     EDTEGNDSES SEDE
//