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Database: UniProt/TrEMBL
Entry: Q2L2T2_BORA1
LinkDB: Q2L2T2_BORA1
Original site: Q2L2T2_BORA1 
ID   Q2L2T2_BORA1            Unreviewed;       883 AA.
AC   Q2L2T2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   02-NOV-2016, entry version 84.
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   ECO:0000313|EMBL:CAJ48956.1};
GN   OrderedLocusNames=BAV1347 {ECO:0000313|EMBL:CAJ48956.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48956.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ48956.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ48956.1,
RC   ECO:0000313|Proteomes:UP000001977};
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: 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:SAAS00075911}.
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:SAAS00565436}.
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DR   EMBL; AM167904; CAJ48956.1; -; Genomic_DNA.
DR   RefSeq; WP_012417028.1; NC_010645.1.
DR   ProteinModelPortal; Q2L2T2; -.
DR   STRING; 360910.BAV1347; -.
DR   EnsemblBacteria; CAJ48956; CAJ48956; BAV1347.
DR   KEGG; bav:BAV1347; -.
DR   PATRIC; 21128886; VBIBorAvi43433_1366.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; EMKSAYI; -.
DR   BioCyc; BAVI360910:GCKI-1358-MONOMER; -.
DR   Proteomes; UP000001977; 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_pinwhl.
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; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00440775};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001977};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454525};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454466, ECO:0000313|EMBL:CAJ48956.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00440785};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454388}.
FT   DOMAIN       11    506       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   MOTIF       571    577       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    122    122       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
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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