(data stored in ACNUC1104 zone)

SWISSPROT: A4F5N8_SACEN

ID   A4F5N8_SACEN            Unreviewed;       831 AA.
AC   A4F5N8;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 89.
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   ECO:0000313|EMBL:CAL99362.1};
GN   OrderedLocusNames=SACE_0009 {ECO:0000313|EMBL:CAL99362.1};
GN   ORFNames=A8924_0390 {ECO:0000313|EMBL:PFG93162.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99362.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99362.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99362.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93162.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93162.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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; AM420293; CAL99362.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93162.1; -; Genomic_DNA.
DR   RefSeq; WP_009945686.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0009; -.
DR   EnsemblBacteria; CAL99362; CAL99362; SACE_0009.
DR   KEGG; sen:SACE_0009; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; SERY405948:SACE_RS00035-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F5N8.
DR   SWISS-2DPAGE; A4F5N8.
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:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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:CAL99362.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   DOMAIN       15    473       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   COILED      445    472       {ECO:0000256|SAM:Coils}.
FT   MOTIF       534    540       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   831 AA;  92498 MW;  88210A27867AA4EB CRC64;
     MTETLPPEHG RIEPVDIQQE MQNSYINYAM SVIVARALPD VRDGLKPVHR RVLYSMYDSG
     YRPDRGYVKC SRVVGDVMGN YHPHGDSSIY DTLVRLAQPW SMRHPLIDGQ GNFGSPGNDP
     AAAMRYTESR LDPLAMHMLA DIEEDTVDFS DNYDGRSQEP DVLPARIPNL LVNGGGGIAV
     GMATNIPPHN LREVADGVVW ALENPEADDE ALLEALIERI KGPDFPTRGL IMGTNAIADA
     YRTGRGSIKM RAVVDVEEDT KGRTSLVVTE LPYQVNPDNL IESIAAMHRE GKLTGISDIA
     DESNSRRGMR IVITLKRDSI PKVVLNNLYK HTQLQYTFGV NMLALVEGVP RTLRLDQVIR
     HYVKHQVEVI VRRTRFRLRK AEERAHILRG LVKALDMLDE VIALIRRSPT VDDARTGLIE
     LLEVDEVQAN AILEMQLRRL AALERQKIVD QLAEIEREIE DLKDILDKPE RQRQIIRDEL
     MAIVDKHGDD RRTRIVPHEG EVSMEDLIAD EDVVVTLTRT GYAKRTRTDL YRAQKRGGKG
     VQGAQLKQDD IVSHFFVCST HDWILFFTNK GRVYRAKAYE LPEANRTARG QHVANLLAFQ
     PDEHIAQVMQ IKDYTAAPYL VLATRNGLVK KSRLTDFDSN RSGGLIGVNL KDDDELVGAV
     LCSADDDLLL VSAEGQSIRF HASDEALRPM GRATSGVLGM RFNEGDELLA MGVVRPDRYV
     LVATDGGYAK RTPIDDYPVQ GRGGKGVLTI QYDRKRGRLV GALIVDVDDE LYAITSTGGV
     IRTTAKEVRK AGRQTKGVRL MNLGDGTSVV AVARNADEAA DPDAAGPEQQ K
//

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