(data stored in ACNUC7421 zone)

SWISSPROT: A8FQA4_SHESH

ID   A8FQA4_SHESH            Unreviewed;       391 AA.
AC   A8FQA4;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631};
GN   Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN   OrderedLocusNames=Ssed_0414 {ECO:0000313|EMBL:ABV35027.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35027.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35027.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35027.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that forms a contractile
CC       ring structure (Z ring) at the future cell division site. The
CC       regulation of the ring assembly controls the timing and the
CC       location of cell division. One of the functions of the FtsZ ring
CC       is to recruit other cell division proteins to the septum to
CC       produce a new cell wall between the dividing cells. Binds GTP and
CC       shows GTPase activity. {ECO:0000256|HAMAP-Rule:MF_00909,
CC       ECO:0000256|RuleBase:RU000631}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|HAMAP-
CC       Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
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DR   EMBL; CP000821; ABV35027.1; -; Genomic_DNA.
DR   RefSeq; WP_012140764.1; NC_009831.1.
DR   ProteinModelPortal; A8FQA4; -.
DR   STRING; 425104.Ssed_0414; -.
DR   EnsemblBacteria; ABV35027; ABV35027; Ssed_0414.
DR   KEGG; sse:Ssed_0414; -.
DR   eggNOG; ENOG4105CDK; Bacteria.
DR   eggNOG; COG0206; LUCA.
DR   HOGENOM; HOG000049094; -.
DR   KO; K03531; -.
DR   OMA; MRAVKGI; -.
DR   OrthoDB; POG091H02KK; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0090529; P:cell septum assembly; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP.
DR   CDD; cd02201; FtsZ_type1; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   HAMAP; MF_00909; FtsZ; 1.
DR   InterPro; IPR000158; Cell_div_FtsZ.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR024757; FtsZ_C.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Pfam; PF12327; FtsZ_C; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   TIGRFAMs; TIGR00065; ftsZ; 1.
DR   PROSITE; PS01134; FTSZ_1; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQA4.
DR   SWISS-2DPAGE; A8FQA4.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631, ECO:0000313|EMBL:ABV35027.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN       13    205       Tubulin. {ECO:0000259|SMART:SM00864}.
FT   DOMAIN      207    325       Tubulin_C. {ECO:0000259|SMART:SM00865}.
FT   NP_BIND      21     25       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   NP_BIND     108    110       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     139    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     143    143       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     187    187       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
SQ   SEQUENCE   391 AA;  40566 MW;  3BB9089953BAE027 CRC64;
     MFEIMDSHTD EAVIKVIGVG GGGGNAIEHM VKHNIEGVEF VATNTDAQAL RKSSAGSTIQ
     LGRDITKGLG AGANPEIGRL AAEEDKENIR NAIKGSDMIF IAAGMGGGTG TGAAPVVAEV
     AKEEGILTVA VVTKPFPFEG KKRMSYADQG IAELAKHVDS LITIPNEKLL KVLGRGTSLL
     DAFAAANNVL LGAVQGIAEL ITRPGLINVD FADVKTVMSE MGNAMMGTGV ASGEDRAEEA
     AEAAVASPLL EDIDLAGARG VLVNITAGMD MSIEEFETVG NHVKAYASDN ATVVVGAVID
     PEMSDELRVT VVATGIGAEK KPDIQLVTKP APRPEPIVTP EVRPETASEE MIAQPMVTGN
     VVPVAQTAPA PAPKNEADYL DIPAFLRKQA D
//

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