(data stored in SCRATCH3701 zone)

HOGENOM6: HELPB_1_PE579

ID   HELPB_1_PE579                        STANDARD;      PRT;   827 AA.
AC   HELPB_1_PE579; C7BZA2;
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; EC=5.99.1 3; (HELPB_1.PE579).
GN   Name=gyrA; OrderedLocusNames=HELPY_0668;
OS   HELICOBACTER PYLORI B38.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=592205;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HELPB_1.PE579.
CC       Helicobacter pylori B38, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7BZA2_HELPB
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; C7BZA2; -.
DR   EMBL; FM991728; CAX29200.1; -; Genomic_DNA.
DR   RefSeq; YP_003057422.1; NC_012973.1.
DR   STRING; C7BZA2; -.
DR   GeneID; 8207854; -.
DR   GenomeReviews; FM991728_GR; HELPY_0668.
DR   KEGG; hpb:HELPY_0668; -.
DR   OMA; TSIPPHR; -.
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:EC.
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; HELPB_1.PE579; -.
DR   PRODOM; HELPB_1_PE579.
DR   SWISS-2DPAGE; HELPB_1_PE579.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   827 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQDRLVNETK NIVEVGIDSS IEESYLAYSM SVIIGRALPD ARDGLKPVHR RILYAMHELG
     LTSKVAYKKS ARIVGDVIGK YHPHGDNAVY DALVRMAQDF SMRLELVDGQ GNFGSIDGDN
     AAAMRYTEAR MTKASEEILR DIDKDTIDFV PNYDDTLKEP DILPSRLPNL LVNGANGIAV
     GMATSIPPHR IDEIIDALAH VLENPNAELD EILEFVKGPD FPTGGIIYGK AGIVEAYKTG
     RGRVKVRAKV HVEKTKNKEI IVLDEMPFQT NKAKLVEQIS DLAREKQIEG ISEVRDESDR
     EGIRVVIELK RDAMSEIVLN HLYKLTTMET TFSIILLAIY NKEPKIFTLL ELLCLFLNHR
     KTIIIRRTIF ELEKAKARAH ILEGYLIALD NIDEIVQLIK TSPSPEAAKN ALMERFTLSE
     IQSKAILEMR LQRLTCLERD KIKEEYQNLL ELIADLNGIL KSEDRLNEVV KIELLEIKEQ
     FSSPRRTEIQ ESYENIDIED LIANEPMVVS MSYKGYVKRV DLKAYEKQNR GGKGKLSGST
     YEDDFIENFF VANTHDILLF ITNKGQLYHL KVYKIPEASR IAMGKAVVNL ISLAPDEKIM
     ATLSTKDFSD ERSLAFFTKN GVVKRTNLSE FGSNRSCGVR AIVLDEGDEL VSAKVVDKNA
     KHLLIASHLG IFIKFPLEDV REMGRNARGV IGIRLNENDF VVGAVVISDD GNKLLSVSEN
     GLGKQTLAEA YREQSRGGKG VIGMKLTQKT GNLVGVISVD DENLDLMILT ASAKMIRVSI
     KDIRETGRNA SGVKLINTAD KVMYVNSCPK EEEPENLETS SAQNLFE
//

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