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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   11-JUN-2014, entry version 32.
DE   RecName: Full=DNA gyrase subunit A;
DE            EC=5.99.1.3;
GN   Name=gyrA; OrderedLocusNames=BPLAN_147;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPLAN;
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: 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; CP001429; ACX83776.1; -; Genomic_DNA.
DR   RefSeq; YP_003256919.1; NC_013418.2.
DR   STRING; 600809.BPLAN_147; -.
DR   EnsemblBacteria; ACX83776; ACX83776; BPLAN_147.
DR   GeneID; 8527879; -.
DR   KEGG; bpi:BPLAN_147; -.
DR   PATRIC; 31960209; VBIBlaSp127104_0148.
DR   eggNOG; COG0188; -.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; MPIKVFR; -.
DR   OrthoDB; EOG661H5V; -.
DR   BioCyc; BSP600809:GHSF-147-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; 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
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    121    121       O-(5'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity){EA8}.
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
//
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