(data stored in ACNUC7421 zone)

SWISSPROT: B7UIE5_ECO27

ID   B7UIE5_ECO27            Unreviewed;       383 AA.
AC   B7UIE5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
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   ECO:0000313|EMBL:CAS07648.1};
GN   OrderedLocusNames=E2348C_0100 {ECO:0000313|EMBL:CAS07648.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07648.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07648.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure
CC       in a strictly GTP-dependent manner. Interacts directly with
CC       several other division proteins. {ECO:0000256|HAMAP-
CC       Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000256|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|HAMAP-
CC       Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
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DR   EMBL; FM180568; CAS07648.1; -; Genomic_DNA.
DR   RefSeq; WP_000462776.1; NC_011601.1.
DR   SMR; B7UIE5; -.
DR   EnsemblBacteria; CAS07648; CAS07648; E2348C_0100.
DR   KEGG; ecg:E2348C_0100; -.
DR   HOGENOM; HOG000049094; -.
DR   KO; K03531; -.
DR   OMA; MRAVKGI; -.
DR   BioCyc; ECOL574521:E2348C_RS00515-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-UniRule.
DR   CDD; cd02201; FtsZ_type1; 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; IPR036525; Tubulin/FtsZ_GTPase_sf.
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; B7UIE5.
DR   SWISS-2DPAGE; B7UIE5.
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:CAS07648.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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       12    204       Tubulin. {ECO:0000259|SMART:SM00864}.
FT   DOMAIN      206    324       Tubulin_C. {ECO:0000259|SMART:SM00865}.
FT   NP_BIND      20     24       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   NP_BIND     107    109       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     138    138       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     142    142       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     186    186       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
SQ   SEQUENCE   383 AA;  40324 MW;  B3A53340367DBBA0 CRC64;
     MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR KTAVGQTIQI
     GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI AAGMGGGTGT GAAPVVAEVA
     KDLGILTVAV VTKPFNFEGK KRMAFAEQGI TELSKHVDSL ITIPNDKLLK VLGRGISLLD
     AFGAANDVLK GAVQGIAELI TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA
     EMAISSPLLE DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP
     DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE QKPVAKVVND
     NAPQTAKEPD YLDIPAFLRK QAD
//

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