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Database: UniProt/TrEMBL
Entry: E3EDT0_PAEPS
LinkDB: E3EDT0_PAEPS
Original site: E3EDT0_PAEPS 
ID   E3EDT0_PAEPS            Unreviewed;       854 AA.
AC   E3EDT0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   06-JUL-2016, entry version 45.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Synonyms=gyrA1 {ECO:0000313|EMBL:ADO53996.1};
GN   ORFNames=PPSC2_00040 {ECO:0000313|EMBL:ADO53996.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO53996.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO53996.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO53996.1,
RC   ECO:0000313|Proteomes:UP000006868};
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: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01897,
CC       ECO:0000256|SAAS:SAAS00075911}.
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_01897}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS00565436}.
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DR   EMBL; CP002213; ADO53996.1; -; Genomic_DNA.
DR   RefSeq; WP_013368650.1; NC_014622.2.
DR   STRING; 886882.PPSC2_c0008; -.
DR   EnsemblBacteria; ADO53996; ADO53996; PPSC2_00040.
DR   GeneID; 25384681; -.
DR   KEGG; ppm:PPSC2_00040; -.
DR   PATRIC; 42503290; VBIPaePol172748_0009.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; ETVDWVP; -.
DR   BioCyc; PPOL886882:GBY1-8-MONOMER; -.
DR   Proteomes; UP000006868; 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-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-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; IPR013760; Topo_IIA-like_dom.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00440775}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006868};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454525};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454466};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00440785};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454388}.
FT   DOMAIN       12    464       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   COILED      417    456       {ECO:0000256|SAM:Coils}.
FT   MOTIF       525    531       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    123    123       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
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
//
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