GenomeNet

Database: UniProt/TrEMBL
Entry: D0J8V5_BLASP
LinkDB: D0J8V5_BLASP
Original site: D0J8V5_BLASP 
ID   D0J8V5_BLASP            Unreviewed;       817 AA.
AC   D0J8V5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   02-NOV-2016, entry version 48.
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:ACX83776.1};
GN   OrderedLocusNames=BPLAN_147 {ECO:0000313|EMBL:ACX83776.1};
OS   Blattabacterium sp. subsp. Periplaneta americana (strain BPLAN)
OS   (Periplaneta americana symbiotic bacterium).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=600809 {ECO:0000313|EMBL:ACX83776.1, ECO:0000313|Proteomes:UP000002225};
RN   [1] {ECO:0000313|EMBL:ACX83776.1, ECO:0000313|Proteomes:UP000002225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPLAN {ECO:0000313|EMBL:ACX83776.1,
RC   ECO:0000313|Proteomes:UP000002225};
RX   PubMed=19880743; DOI=10.1073/pnas.0907504106;
RA   Sabree Z.L., Kambhampati S., Moran N.A.;
RT   "Nitrogen recycling and nutritional provisioning by Blattabacterium,
RT   the cockroach endosymbiont.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001429; ACX83776.1; -; Genomic_DNA.
DR   RefSeq; WP_012821304.1; NC_013418.2.
DR   STRING; 600809.BPLAN_147; -.
DR   EnsemblBacteria; ACX83776; ACX83776; BPLAN_147.
DR   KEGG; bpi:BPLAN_147; -.
DR   PATRIC; 31960209; VBIBlaSp127104_0148.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; EMKSAYI; -.
DR   OrthoDB; POG091H025U; -.
DR   Proteomes; UP000002225; 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; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; -; 2.
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   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:UP000002225};
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};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00440785};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00454388}.
FT   DOMAIN       10    462       TOP4c. {ECO:0000259|SMART:SM00434}.
FT   MOTIF       523    529       GyrA-box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01897}.
FT   ACT_SITE    121    121       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01897}.
SQ   SEQUENCE   817 AA;  93699 MW;  DB216B5D84C3AA00 CRC64;
     MNEGEKLIPI NIEDEMKSSY IDYSMSVIVS RALPDARDGL KPVHRRVLYG MYQLGIFSNN
     PYKKSARIVG EVLGKYHPHG DISVYETMVR MAQKWTLRYP LIDGQGNFGS LDADPPAAMR
     YTEVRMKKMS EEMLLDIKKE TVDMQLNFDD SIEEPTVLPT RIPNLLINGS SGIAVGMATN
     IPPHNLKETI KAIFAYIEND QISIEQIMEY IKAPDFPTGG IIYGYEGVKK AFYTGRGRIV
     LRAKVHLEEI QGRQCIIVDE IPYQVNKAEM ITRTVELMRE GKMEGIYQIR DESDRNGLRI
     VYLLKQNTNP HILLNNLFKY TSLQTYFNVN NIALVKGKPV QLNIKDLIQH FVDHRQDVII
     RRTKYELKKC QDRIHTLTGF LTILDHLDKM IELIKESKDH HEACNRLIKM FKLSENQSRS
     ILDMRLQNLT SLELKKIKKE YEELVKKIAY LKNVLIQHSI RMQIIKKELL DIQDKYQDKR
     RTQIDYLGNE VHIEDLIEDE QVVLTISHAG YIKRTSLSEY KRQGRGGIGN RGASARESDF
     FKHLLIATNH QYLLFFTEKG KCFWLRVYEI PEGSKISKGR AIQNMIHLQP DDKVNAYILT
     GDLTNKKYVQ NHYVMMVTQK GIIKKTSLEN YSRPRKDGIN AIVIRKGDSL LEAILTKGNS
     HVFIAVKSGK IIRFSEKKVR ATGRNSSGVR GINLSISEDT VIGMICVEGQ EKGYLLVVSE
     KGFGKRTNLK DYRITNRGGK GIKTINITQK TGSLISIKHV TNQDDLMIIK KSGIIIRISV
     SDIRVMGRDT QGVRLINLKE KDEIADVEKV SQTMDFH
//
DBGET integrated database retrieval system