(data stored in SCRATCH3701 zone)

HOGENOM6: BIFBS_1_PE6

ID   BIFBS_1_PE6                          STANDARD;      PRT;   910 AA.
AC   BIFBS_1_PE6; E3END2;
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=GyrA1 DNA gyrase subunit A; (BIFBS_1.PE6).
GN   Name=gyrA1; OrderedLocusNames=BBIF_0005;
OS   BIFIDOBACTERIUM BIFIDUM S17.
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=883062;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BIFBS_1.PE6.
CC       Bifidobacterium bifidum S17 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E3END2_BIFBS
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; E3END2; -.
DR   EMBL; CP002220; ADO52210.1; -; Genomic_DNA.
DR   RefSeq; YP_003937784.1; NC_014616.1.
DR   GeneID; 9846195; -.
DR   GenomeReviews; CP002220_GR; BBIF_0005.
DR   KEGG; bbi:BBIF_0005; -.
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:InterPro.
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; BIFBS_1.PE6; -.
DR   PRODOM; BIFBS_1_PE6.
DR   SWISS-2DPAGE; BIFBS_1_PE6.
KW   gyrA1 DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   910 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADENSNGTD LPEQNDERAE HSMEPISPQA NEQLVLDDNR VAHTDIQKEM RQSYLDYAIS
     VIVERALPDV RDGMKPVHRR IVYAMYDGGY RPDRGYSKCA RPVADVMGNY HPHGDAAIYD
     SLVRMAQPWS MRYTLVDGQG NFGSAGDDPP AAMRYTECRM MPLAMEMVRD IDKDTVDFVP
     NYDGRTQEPT VLPARFPNLL ANGSSGIAVG MATNIPPHNM RELAEGVHWT LDHPEASHEE
     LLNALIGIIK GPDFPTGATI LGHKGIEQAY RTGRGLITMR AVVNTEEIKG RMCLVVTELP
     YQVNPDRLAA SIREGVRDGK IQGIADMRDE TSGRTGQRLV LVLKRDAVPK VVLNNLYKHS
     QLQQTFGANM LALVDGVPRT LSLDAFIRHW VNHQLEVIER RTRYLKREAE ERDHILQGLL
     KAMDAIDEII RLIRSSQGRE DARPKLMEFL DIDQVQADAI LSMQLVRLAN MERQKIIDEH
     EELMRKIADY NDILAKPERQ RTIVGDELDE IVAKYGDERR TKILPYSGEM NVEDLIAEEN
     VVVTVTHSGF IKRTKANEYR AQHRGGKGIK GAKLREDDVV DHFFLTSTHN WLLFFTNKGR
     VYRIKAYELP EGSRDSKGQH VANLLQFGPD ETIQTVLSIP NYEVAKYLVL ATRTGKVKKT
     ALAEYDSPRQ GGLIAVRLAA DEETGEPTDE LIGAALCNAA DDIILVSKQG MSLKFAADND
     QLRPMGRQTA GVQGMKFRGD DELLAMDVVP EDSKQDLLVV TNEGFAKRTA ISEYRLQGRN
     GFGVKAVQLA EGRGSLVGAL IVSEDDQVMA IMKSGKVIRS NVTEVKRTGR TTQGVTLAKP
     DKGDEIISIA RNEETGEDEV ETTDDTAAAA SATTSPDTAE NTPDTTDSVA SGSDSGAASD
     ENVNNTDDEA
//

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