(data stored in ACNUC7421 zone)

HOGENOM: MITES1_1_PE100

ID   MITES1_1_PE100                       STANDARD;      PRT;   395 AA.
AC   MITES1_1_PE100; E8N844;
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   RecName: Full=Cell division protein ftsZ; (MITES1_1.PE100).
GN   Name=ftsZ; OrderedLocusNames=MTES_0100;
OS   MICROBACTERIUM TESTACEUM STLB037.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Microbacterium.
OX   NCBI_TaxID=979556;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MITES1_1.PE100.
CC       Microbacterium testaceum StLB037, complete genome.
CC       1..405839 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E8N844_MICTS
CC   -!- FUNCTION: This protein is essential to the cell-division process.
CC       It seems to assemble into a dynamic ring on the inner surface of
CC       the cytoplasmic membrane at the place where division will occur,
CC       and the formation of the ring is the signal for septation to
CC       begin. Binds to and hydrolyzes GTP (By similarity).
CC   -!- SUBUNIT: Aggregates to form a ring-like structure (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ftsZ family.
CC   -!- GENE_FAMILY: HOG000049094 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E8N844; -.
DR   EMBL; AP012052; BAJ73064.1; -; Genomic_DNA.
DR   RefSeq; YP_004222944.1; NC_015125.1.
DR   GeneID; 10217118; -.
DR   GenomeReviews; AP012052_GR; MTES_0100.
DR   KEGG; mts:MTES_0100; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043234; C:protein complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0000917; P:barrier septum formation; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR000158; Cell_div_FtsZ_N.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   TIGRFAMs; TIGR00065; FtsZ; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
DR   HOGENOMDNA; MITES1_1.PE100; -.
KW   cell division GTPase;
KW   Cell cycle; Cell division; Complete proteome; GTP-binding;
KW   Nucleotide-binding; Septation.
SQ   SEQUENCE   395 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSHNQNYLAV IKVVGVGGGG VNAVNRMIEL GLRGVEFIAI NTDAQALLMS DADVKLDVGR
     ELTRGLGAGA DPEVGRRAAE DHAEEIEEAL RGADMVFVTA GEGGGTGTGG APVVAKIAKS
     IGALTIGVVT KPFSFEGRRR QSQAEAGVGR LKEEVDTLIV VPNDRLLEIS DRGISMIEAF
     ATADQVLLAG VQGITDLITT PGLINLDFAD VKSVMQGAGS ALMGIGSARG ADRAIKAAEL
     AVESPLLEAS IEGAHGVLLS IQGGSNLGIF EINDAAQLVK EAAHPEANII FGTVIDDTLG
     DEVRVTVIAA GFDGGEPSLR IDAVGAQRAV SAPVVPVIPA DDVARDLHAA EEQKASTERA
     PERKPEPAPV AAHVPESSYD GGFADDDLDV PDFLK
//

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