(data stored in SCRATCH3701 zone)

HOGENOM6: CHLP8_1_PE95

ID   CHLP8_1_PE95                         STANDARD;      PRT;   826 AA.
AC   CHLP8_1_PE95; B3QRK9;
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, A subunit; EC=5.99.1 3; (CHLP8_1.PE95).
GN   OrderedLocusNames=Cpar_0096;
OS   CHLOROBACULUM PARVUM NCIB 8327.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLP8_1.PE95.
CC       Chlorobaculum parvum NCIB 8327 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B3QRK9_CHLP8
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; B3QRK9; -.
DR   EMBL; CP001099; ACF10524.1; -; Genomic_DNA.
DR   RefSeq; YP_001997724.1; NC_011027.1.
DR   STRING; B3QRK9; -.
DR   GeneID; 6418997; -.
DR   GenomeReviews; CP001099_GR; Cpar_0096.
DR   KEGG; cpc:Cpar_0096; -.
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: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; CHLP8_1.PE95; -.
DR   PRODOM; CHLP8_1_PE95.
DR   SWISS-2DPAGE; CHLP8_1_PE95.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   826 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQREKILPIS IEEEMRDAYL DYSMSVIVSR ALPDVRDGLK PVHRRVLYGM HELGLQSNKP
     HKKSARVVGE VLGKYHPHGD SAVYDSLVRM VQDFSLRYPL IDGQGNFGSV DGDSPAAMRY
     TEVRMKAIAG EMLKDLDKET VDFALNFDDS LEEPTVLPSA IPNLLVNGAS GIAVGMATNI
     PPHNMREVVS GLIAMIDDPE IEITDLMKYV TAPDFPTGGI IYGYEGVRQA YLTGRGKVVI
     RARAVVEVTQ KNGRESIIVT ELPYQVNKVR LIEKIVELVH DKKIEGIADI RDESDREGMR
     LVIELKRDAV PKVVLNHLYK HTPMQDTFGV IMLALVDGVP RVLNLKEMMQ YYIRHRNEIV
     LRRTQYDLNA AEKRAHILEG LKICLDNLDE VITTIRQSPD TPTAQSRLID RFGLTEVQAK
     AILEMRLQRL TGMERQKIDD EYKQTMALIE ELKSILASPA KQMEIIKEEL LKVSEVYGDE
     RRTEMRPQEG DFSIEDMIAQ EDVVITITHD GFIKRFPVSG YRRQHRGGRG VAGAQAKNED
     FIEHMFIAST HNYILFFTTA GRCYWLKVYE IPEAGRSARG RSLANIMELP PGEKIRTYIN
     IRNFDDPHFI IMATANGIVK KTDLKQYSNP RRTGINAITI EEGDELIEAR LTDGDHQVIL
     AKSSGYAVRF PESEVRSMGR TAMGVKGITL DEAERCISMV TTKRNDTSLL AVTDNGYGKR
     SKVEDYRMTK RGARGVITIK AHEKIGNLVG LLDVNDEDDL IIITTNGIVI RQHVSDIRVL
     GRNTSGVRLI RLDAGDRISA TARVPKSDDE PTSEPLGEDG QIDMGF
//

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