FTSZ_AQUAE
ID FTSZ_AQUAE Reviewed; 367 AA.
AC O66809;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=aq_525;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-331 IN COMPLEX WITH GDP.
RX PubMed=17900614; DOI=10.1016/j.jmb.2007.08.056;
RA Oliva M.A., Trambaiolo D., Lowe J.;
RT "Structural insights into the conformational variability of FtsZ.";
RL J. Mol. Biol. 373:1229-1242(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-331.
RX PubMed=18291323; DOI=10.1016/j.chembiol.2007.12.013;
RA Lappchen T., Pinas V.A., Hartog A.F., Koomen G.J., Schaffner-Barbero C.,
RA Andreu J.M., Trambaiolo D., Lowe J., Juhem A., Popov A.V., den Blaauwen T.;
RT "Probing FtsZ and tubulin with C8-substituted GTP analogs reveals
RT differences in their nucleotide binding sites.";
RL Chem. Biol. 15:189-199(2008).
CC -!- FUNCTION: Essential cell division protein that forms a contractile ring
CC structure (Z ring) at the future cell division site. The regulation of
CC the ring assembly controls the timing and the location of cell
CC division. One of the functions of the FtsZ ring is to recruit other
CC cell division proteins to the septum to produce a new cell wall between
CC the dividing cells. Binds GTP and shows GTPase activity.
CC {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC strictly GTP-dependent manner. Interacts directly with several other
CC division proteins. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; AE000657; AAC06771.1; -; Genomic_DNA.
DR PIR; E70347; E70347.
DR RefSeq; NP_213369.1; NC_000918.1.
DR RefSeq; WP_010880307.1; NC_000918.1.
DR PDB; 2R6R; X-ray; 1.70 A; 1=1-331.
DR PDB; 2R75; X-ray; 1.40 A; 1=1-331.
DR PDBsum; 2R6R; -.
DR PDBsum; 2R75; -.
DR AlphaFoldDB; O66809; -.
DR SMR; O66809; -.
DR STRING; 224324.aq_525; -.
DR BindingDB; O66809; -.
DR EnsemblBacteria; AAC06771; AAC06771; aq_525.
DR KEGG; aae:aq_525; -.
DR PATRIC; fig|224324.8.peg.431; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_0; -.
DR InParanoid; O66809; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR EvolutionaryTrace; O66809; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
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; 3.30.1330.20; -; 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; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..367
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114338"
FT BINDING 17..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:17900614"
FT BINDING 104..106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:17900614"
FT BINDING 135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:17900614"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:17900614"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 175..198
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:2R75"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2R75"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2R75"
SQ SEQUENCE 367 AA; 40161 MW; 0DEC8A6A865348A9 CRC64;
MEEFVNPCKI KVIGVGGGGS NAVNRMYEDG IEGVELYAIN TDVQHLSTLK VPNKIQIGEK
VTRGLGAGAK PEVGEEAALE DIDKIKEILR DTDMVFISAG LGGGTGTGAA PVIAKTAKEM
GILTVAVATL PFRFEGPRKM EKALKGLEKL KESSDAYIVI HNDKIKELSN RTLTIKDAFK
EVDSVLSKAV RGITSIVVTP AVINVDFADV RTTLEEGGLS IIGMGEGRGD EKADIAVEKA
VTSPLLEGNT IEGARRLLVT IWTSEDIPYD IVDEVMERIH SKVHPEAEII FGAVLEPQEQ
DFIRVAIVAT DFPEEKFQVG EKEVKFKVIK KEEKEEPKEE PKPLSDTTYL EEEEIPAVIR
RKNKRLL
