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Entry: Q2L2T2_BORA1
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ID   Q2L2T2_BORA1            Unreviewed;       883 AA.
AC   Q2L2T2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   11-JUN-2014, entry version 63.
DE   RecName: Full=DNA gyrase subunit A;
DE            EC=5.99.1.3;
GN   Name=gyrA; OrderedLocusNames=BAV1347;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       Within the heterotetramer, GyrA contains the active site tyrosine
CC       that forms a covalent intermediate with the DNA, while GyrB
CC       contributes the cofactor binding sites and catalyzes ATP
CC       hydrolysis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
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DR   EMBL; AM167904; CAJ48956.1; -; Genomic_DNA.
DR   RefSeq; YP_785869.1; NC_010645.1.
DR   ProteinModelPortal; Q2L2T2; -.
DR   SMR; Q2L2T2; 30-532, 547-853.
DR   STRING; 360910.BAV1347; -.
DR   GeneID; 6267458; -.
DR   KEGG; bav:BAV1347; -.
DR   PATRIC; 21128886; VBIBorAvi43433_1366.
DR   eggNOG; COG0188; -.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; ASAKMIR; -.
DR   OrthoDB; EOG661H5V; -.
DR   BioCyc; BAVI360910:GCKI-1371-MONOMER; -.
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:InterPro.
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_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_like_dom.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01063; gyrA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
FT   ACT_SITE    122    122       O-(5'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity){EA12}.
SQ   SEQUENCE   883 AA;  97906 MW;  ED9D0959553B92E1 CRC64;
     MDSFAKETLP VSLEEEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMHELNNDWN
     RAYKKSARIV GDVIGKYHPH GDQSVYDTIV RMAQDFSMRY MLVDGQGNFG SIDGDNAAAM
     RYTEIRLAKI AHELLADIDQ ETVDFGPNYD GSEQEPLLLP SRLPNLLVNG SSGIAVGMAT
     NIPPHNLGEV VEGCLYCLRN PECTIDELLE IIPAPDFPTG GIIYGMVGVR EGYRTGRGRV
     IMRAKTHFED MDKGNRQAIV VDAIPYQVNK KTLQERIAEL VNEKKIEGIS DIRDESDKDG
     MRLVIELKRG EVPEVVLNNL YKNTQLQDTF GMNLVALVDG QPRLLNLKQL ISYFLQHRRE
     VVTRRTVFQL RKARERGHVL EGLAVALANI DDFIAIIKAA PTPPVARQEL MARNWDSSLV
     REMLARADGD VVGGRQAFRP EDLPEGFGLQ GDGQYRLSET QAQEILNMRL QRLTGLEQDK
     IIGEYKDVMD TIADLLDILA RPERITTIIG EELQAIKAEF SSGAKDSRRS EIELNATELD
     TEDLITPMDM VVTMSHGGYI KSQPLSEYRS QKRGGRGKQA TQMKENDWVD QLFIANTHDY
     LLCFSNRGRV YWLKVWEVPQ GTRNSRGKPI VNMFPLADGE KITVVLPVKE FSDDHYVFMA
     TSRGTVKKTA LSDFSNPRKA GIIAVDLDEG DYLIGADLTD GKHDVMLFSD SGKAVRFDEN
     DVRPMGRAAR GVRGMMLEDS QSVIALLVAG DESQSVLTAT ENGYGKRTSI AEYTRHGRGT
     KGMIAIQTSS RNGRVVGAVL VNPSDEIMLI TTGGVLVRTR VSEIREMGRA TQGVTLISVD
     DGSSLSGVRR VAESDADDDE AADAADGSDG ADGVAESTEE PTE
//
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