(data stored in ACNUC7421 zone)

SWISSPROT: E3J256_FRAIE

ID   E3J256_FRAIE            Unreviewed;       830 AA.
AC   E3J256;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE            EC=5.6.2.3 {ECO:0000256|HAMAP-Rule:MF_01897};
GN   Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN   OrderedLocusNames=FraEuI1c_0006 {ECO:0000313|EMBL:ADP78094.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78094.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78094.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01897, ECO:0000256|SAAS:SAAS01173059};
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:SAAS01062860}.
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DR   EMBL; CP002299; ADP78094.1; -; Genomic_DNA.
DR   RefSeq; WP_013421217.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0006; -.
DR   EnsemblBacteria; ADP78094; ADP78094; FraEuI1c_0006.
DR   KEGG; fri:FraEuI1c_0006; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; FSP298654:G1GOT-6-MONOMER; -.
DR   Proteomes; UP000002484; 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
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;
DR   PRODOM; E3J256.
DR   SWISS-2DPAGE; E3J256.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062880}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00972514, ECO:0000313|EMBL:ADP78094.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN       15    472       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   COILED      444    464       {ECO:0000256|SAM:Coils}.
FT   MOTIF       533    539       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    126    126       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
SQ   SEQUENCE   830 AA;  91675 MW;  6346F31EE9E29DAE CRC64;
     MVDVLPPPGD RIEPIGIEVE MQRSYLDYAM SVIVGRALPE VRDGLKPVHR RVLYAMYDGG
     YRPDRGYFKC SRIVGDVMGN YHPHGDTSIY DTVVRLAQPW SLRYPLVDGN GNFGSPGNDP
     PAAMRYTEAR MAALAMEMLR DIDSDTVDFA PNYDGRSQEP LVLPSRFPNL LVNGAGGIAV
     GMATNIPPHN LREVAAGVQW ALNNPDATDE ELLEALLGII KGPDFPTHGM IVGRQGIEDA
     YRTGRGSIRM RAVVNVEENK GRTQLVVTEL PYQVNPDNLA EKIAELVRDN RISGISDVRD
     ETSARIGQRL VIDLKRDAVA KVVLNNLYKH TQLQDTFGAN MLAIVDGVPR TLRLDQMIRY
     YVEHQVDVIV RRTRYQLRKA QERLHVLEGL LIALDHLDDV IALIRNAESA DAARGQLMTR
     YSLSEIQATA ILDMQLRRLA ALERQRIIDE AAELRAKVTE LEAILASPQR QREIIGEELK
     EVVDKFGDER RTRIVPFEGE MSIEDLIAQE DVVVTVTRGG YAKRTKTDLY RSQKRGGKGV
     QGAALREDDI VEHFFVTTTH HYLLFFTNKG RVYRAKAHEL PEQARSAKGQ HVANILAFGQ
     DERIAEVMAI RDYAAAPYLV LATKRGLCKK SALTDFDSNR AGGLVAINLR EDDEVIGARL
     VGADDDLLLV SRNAQSIRFH ADDEQLRPMG RATAGVIGMR FDADDELLSI EVIKPDSTAS
     LLVATSGGFA KRTHLNEYPL QGRGGKGVLT ARIVPSRGNL VGALVVEPDD QLYAIASNGG
     VLRTVARDVR QAQRQTMGVK LIDLETGVQV VGVARNADAD DGDGDEPTAG
//

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