ID   FTSZ_AZOVI     STANDARD;      PRT;   394 AA.
AC   P77817;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Cell division protein ftsZ.
GN   Name=ftsZ;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=DJ116;
RX   MEDLINE=98267010; PubMed=9605973;
RX   DOI=10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.3.CO;2-Z;
RA   Lu C., Stricker J., Erickson H.P.;
RT   "FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga
RT   maritima -- quantitation, GTP hydrolysis, and assembly.";
RL   Cell Motil. Cytoskeleton 40:71-86(1998).
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.
CC   -!- SUBUNIT: Aggregates to form a ring-like structure.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic. Assembles at the inner surface
CC       of the cytoplasmic membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the ftsZ family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U65939; AAC24603.1; -.
DR   HSSP; P47204; 1OFU.
DR   InterPro; IPR000158; FtsZ.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR003008; Tubulin_FtsZ.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   TIGRFAMs; TIGR00065; ftsZ; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
KW   Cell division; GTP-binding; Septation.
FT   NP_BIND     104    112       GTP (Potential).
SQ   SEQUENCE   394 AA;  41153 MW;  6E3CF750BFA32EAD CRC64;
     MFELVDNVPQ SAVIKVIGVG GGGGNAVNHM AATSIEGIEF ICANTDAQAL KNITARTVLQ
     LGSGVTKGLG AGANPEVGRE AAMEDRERIA EVLQGTDMVF ITTGMGGGTG TGAAPVIAEV
     AKGLGILTVA VVTRPFPFEG RKRMQVAEEG IRLLAEHVDS LITIPNEKLL TILGKDASLL
     SAFAKADDVL AGAVRGISDI IKLSGMINVD FADVKTVMSE MGMAMMGTGF ASGPNRAREA
     TEAAIRNPLL EDVHLQGARG ILVNITAGPD LSLGEYSDVG NIIEQFASDQ AMVKVGTVID
     PDMRDELHVT VVATGLGTRA DKPMKVVDNT LQPAGAAAAA PAVPRGDQTV NYKDYERPTV
     QRQSHAASAT AAKINPQDDL DYLDIPAFLR RQAD
//