(data stored in SCRATCH zone)

SWISSPROT: C6WCG0_ACTMD

ID   C6WCG0_ACTMD            Unreviewed;       840 AA.
AC   C6WCG0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 58.
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   OrderedLocusNames=Amir_0007 {ECO:0000313|EMBL:ACU33981.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU33981.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU33981.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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:SAAS00846455}.
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:SAAS00846457}.
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DR   EMBL; CP001630; ACU33981.1; -; Genomic_DNA.
DR   RefSeq; WP_012782644.1; NC_013093.1.
DR   STRING; 446462.Amir_0007; -.
DR   EnsemblBacteria; ACU33981; ACU33981; Amir_0007.
DR   KEGG; ami:Amir_0007; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; POG091H025U; -.
DR   Proteomes; UP000002213; 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; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_01897; GyrA; 1.
DR   InterPro; IPR024946; Arg_repress_C-like.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR013760; Topo_IIA-like_dom.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_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;
DR   PRODOM; C6WCG0.
DR   SWISS-2DPAGE; C6WCG0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846465};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846460};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846445, ECO:0000313|EMBL:ACU33981.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846452};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00846490}.
FT   DOMAIN       19    477       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   MOTIF       538    544       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    130    130       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
SQ   SEQUENCE   840 AA;  93359 MW;  A740C36F740F6673 CRC64;
     MSETTLPPIG GGSDRTEPRD LQQEMQNSYI DYAMSVIVGR ALPDVRDGLK PVHVRVLYSM
     FDSRFLPERS YNKCARVVGD VMGNYHPHGD SAIYDALVRL AQPWAMRYPL IDGQGNFGSQ
     GNDPAAAMRY TECRLTPLAM RMLADIEEDT VDFRDNYDGR IQEPTVLPSR VPNLLINGSS
     GIAVGMATNI PPHNLREVAE GVVWALDNPE ASDEETLEAM IARIKGPDFP TYGQILGTQG
     IEDAYRTGRG SVKMRAVVEM DEDAKGRTIL VVSELPYQVN PDNLVENIAS LVRDQKINGI
     SNIADESNRR SGMRIVVTVK RDAVAKVVLN NLYKHTQLQY SFGVNMLSLV DGVPRTLRLD
     QMIRHYVKHQ IEVIVRRTKF RLRKAEERAH VWRGLVKALD QLDAVIALIR RSDTTESARS
     GLMELLSVDE VQSNAILEMQ LRRLAALERQ KIIDQLAEIE LQIADLKDIL AKPERQRAIV
     RGELLEIVDK HGDDRRTKIV PFDGDVSMED LIAVEDVVVT ITRTGYAKRT KTDLYRAQKR
     GGKGVQGAQL KQDDIVQHFF VCSTHDWILF FTNKGRVYRT KAYDLPEASR NARGQHVANL
     LAFQPDEEIA QVIQIKNYEA APYLVLATRN GLVKKSKLSD FDSNRSGGLI GINLREEDEL
     VGAVLTGEGD DLLLVSKDGQ SIRFHSSDDV LRPMGRATSG VQGMRFNSDD ELLSMGVVQE
     GLFVLVATDG GYAKRTPIED YPVQGRGGKG VLTIQHDRRR GRLVGALIVD VEDELYAITS
     AGGVIRTSAK EIRKAGRQTK GVRLMNLGEK STLIAVARNA DEPADVSTGE EDDQAIEPAN
//

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