(data stored in SCRATCH3701 zone)

HOGENOM6: MACCJ_5_PE9

ID   MACCJ_5_PE9                          STANDARD;      PRT;   879 AA.
AC   MACCJ_5_PE9; B9E905;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=DNA gyrase subunit A; (MACCJ_5.PE9).
GN   Name=gyrA; OrderedLocusNames=MCCL_0009;
OS   MACROCOCCUS CASEOLYTICUS JCSC5402.
OC   Bacteria; Firmicutes; Bacillales; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MACCJ_5.PE9.
CC       Macrococcus caseolyticus JCSC5402, complete genome.
CC       7988156..8543970 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B9E905_MACCJ
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: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B9E905; -.
DR   EMBL; AP009484; BAH16716.1; -; Genomic_DNA.
DR   RefSeq; YP_002559412.1; NC_011999.1.
DR   STRING; B9E905; -.
DR   GeneID; 7389877; -.
DR   GenomeReviews; AP009484_GR; MCCL_0009.
DR   KEGG; mcl:MCCL_0009; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
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; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
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.
DR   HOGENOMDNA; MACCJ_5.PE9; -.
DR   PRODOM; MACCJ_5_PE9.
DR   SWISS-2DPAGE; MACCJ_5_PE9.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   879 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MALDHDSKLK EQNIVKEMKD SFLDYAMSVI VSRALPDVRD GMKPVHRRIL YGMNNQGMTP
     DKPYKKSARI VGDVMGKYHP HGDSSIYEAM VRMAQDFSYR YMLVDGQGNF GSMDGDGAAA
     MRYTEARMSK IAMELMRDIN KDTIDFTDNY DGNEREPVVL PSRFPNLLVN GASGIAVGMA
     TNIPPHNLTE VINGVLELSK NPDISIPELM ELIQGPDFPT AGLILGRSGI RRAYETGRGS
     VIMRAKTLIE TRPNGKETII ISEIPYQVNK ARLVEKIAEL ARDKKVDGIT DLRDETSLKE
     GVRIVIDVRR DANANVILNN LYKQTPLQTS FGVNMLALVD GKPQVLNIKQ AIYHYLEHQK
     TVVRRRTAYN LKKAEDRAHI LEGLRIALDH IDEIIALIRA SNNDAEALQG LQEQFKLSER
     QAQAILDMRL RRLTGLERDK IESEYQELLK YIDELRAILA DEEKLLQIIR EELIEIRDKY
     GDERRTEIVA GGLEDLEDED LIDEENIVIT LSSNNYIKRL PASTYRAQHR GGRGIQGMNT
     LDEDFVSQMV TTSTHDNVLF FTNKGRVYKV KGYEIPELSR QSKGIPIVNV IDLDKDESIS
     TMIAVKNLER EDAYIVFATK HGLIKRSNLS HFSRINKNGK IAINFREEDE LIAVRLTDGN
     KQLIIGTKHA SLIRFEENKL RPLGRTAAGV KGISLREGDE VIGLDVIESN DEHEVLVVTE
     NGYGKRTKES EYRISNRGGK GIKTATITEK NGNLVCITTV NGNEDIMIVT DHGVIIRLDV
     AEFSQNGRSA QGVRLIRLDE GQFVATVAKV EKEEEVMDED KEPGEVIAEQ GADLTEVAKE
     SIDETIEVED GHVMGTVDVS EQNLLERSEF ESIYNDSEE
//

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