FTSZ_STAA8
ID FTSZ_STAA8 Reviewed; 390 AA.
AC Q2FZ89;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN OrderedLocusNames=SAOUHSC_01150;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9287029; DOI=10.1128/jb.179.17.5632-5635.1997;
RA Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RT "Identification and characterization of cell wall-cell division gene
RT clusters in pathogenic Gram-positive cocci.";
RL J. Bacteriol. 179:5632-5635(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION.
RX PubMed=14617148; DOI=10.1046/j.1365-2958.2003.03719.x;
RA Pinho M.G., Errington J.;
RT "Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence
RT of the division machinery.";
RL Mol. Microbiol. 50:871-881(2003).
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, ECO:0000269|PubMed:14617148}.
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; U94706; AAC45629.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30260.1; -; Genomic_DNA.
DR RefSeq; WP_000888997.1; NZ_LS483365.1.
DR RefSeq; YP_499692.1; NC_007795.1.
DR PDB; 5H5G; X-ray; 2.20 A; A/B=12-316.
DR PDB; 5H5H; X-ray; 1.70 A; A=12-316.
DR PDB; 5H5I; X-ray; 1.90 A; A=12-316.
DR PDB; 5XDT; X-ray; 1.30 A; A=12-316.
DR PDB; 5XDU; X-ray; 2.00 A; A=12-316.
DR PDB; 5XDV; X-ray; 1.70 A; A=12-316.
DR PDB; 5XDW; X-ray; 2.00 A; A=12-316.
DR PDB; 6RVM; X-ray; 2.15 A; A/B/C/D=12-316.
DR PDB; 6RVN; X-ray; 1.24 A; A=12-315.
DR PDB; 6RVP; X-ray; 1.16 A; A=12-315.
DR PDB; 6RVQ; X-ray; 1.14 A; A=12-315.
DR PDB; 6SI9; X-ray; 1.90 A; A=12-316.
DR PDB; 6YD1; X-ray; 1.70 A; A=12-315.
DR PDB; 6YD5; X-ray; 1.55 A; A=12-315.
DR PDB; 6YD6; X-ray; 1.70 A; A=12-315.
DR PDB; 7OHH; X-ray; 1.45 A; A=12-316.
DR PDB; 7OHK; X-ray; 1.75 A; A=12-316.
DR PDB; 7OHL; X-ray; 1.75 A; A=12-316.
DR PDB; 7OHN; X-ray; 1.62 A; A=12-316.
DR PDB; 7OI2; X-ray; 1.90 A; A=12-316.
DR PDB; 7OJA; X-ray; 2.22 A; A=12-316.
DR PDB; 7OJB; X-ray; 1.70 A; A=12-316.
DR PDB; 7OJC; X-ray; 1.95 A; A=12-316.
DR PDB; 7OJD; X-ray; 1.82 A; A=12-316.
DR PDB; 7OJZ; X-ray; 1.65 A; A=12-316.
DR PDB; 7OMJ; X-ray; 1.57 A; A=12-316.
DR PDB; 7OMP; X-ray; 1.52 A; A=12-316.
DR PDB; 7OMQ; X-ray; 1.45 A; A=12-316.
DR PDB; 7ON2; X-ray; 1.69 A; A=12-316.
DR PDB; 7ON3; X-ray; 2.32 A; A=12-316.
DR PDB; 7ON4; X-ray; 1.79 A; A=12-316.
DR PDBsum; 5H5G; -.
DR PDBsum; 5H5H; -.
DR PDBsum; 5H5I; -.
DR PDBsum; 5XDT; -.
DR PDBsum; 5XDU; -.
DR PDBsum; 5XDV; -.
DR PDBsum; 5XDW; -.
DR PDBsum; 6RVM; -.
DR PDBsum; 6RVN; -.
DR PDBsum; 6RVP; -.
DR PDBsum; 6RVQ; -.
DR PDBsum; 6SI9; -.
DR PDBsum; 6YD1; -.
DR PDBsum; 6YD5; -.
DR PDBsum; 6YD6; -.
DR PDBsum; 7OHH; -.
DR PDBsum; 7OHK; -.
DR PDBsum; 7OHL; -.
DR PDBsum; 7OHN; -.
DR PDBsum; 7OI2; -.
DR PDBsum; 7OJA; -.
DR PDBsum; 7OJB; -.
DR PDBsum; 7OJC; -.
DR PDBsum; 7OJD; -.
DR PDBsum; 7OJZ; -.
DR PDBsum; 7OMJ; -.
DR PDBsum; 7OMP; -.
DR PDBsum; 7OMQ; -.
DR PDBsum; 7ON2; -.
DR PDBsum; 7ON3; -.
DR PDBsum; 7ON4; -.
DR AlphaFoldDB; Q2FZ89; -.
DR SMR; Q2FZ89; -.
DR STRING; 1280.SAXN108_1184; -.
DR EnsemblBacteria; ABD30260; ABD30260; SAOUHSC_01150.
DR GeneID; 3920710; -.
DR KEGG; sao:SAOUHSC_01150; -.
DR PATRIC; fig|93061.5.peg.1055; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_9; -.
DR OMA; GNPSIGQ; -.
DR PRO; PR:Q2FZ89; -.
DR Proteomes; UP000008816; 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..390
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000291778"
FT REGION 315..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 108..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:6YD5"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6YD5"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:6YD5"
SQ SEQUENCE 390 AA; 41037 MW; A1E97FCC5C232440 CRC64;
MLEFEQGFNH LATLKVIGVG GGGNNAVNRM IDHGMNNVEF IAINTDGQAL NLSKAESKIQ
IGEKLTRGLG AGANPEIGKK AAEESREQIE DAIQGADMVF VTSGMGGGTG TGAAPVVAKI
AKEMGALTVG VVTRPFSFEG RKRQTQAAAG VEAMKAAVDT LIVIPNDRLL DIVDKSTPMM
EAFKEADNVL RQGVQGISDL IAVSGEVNLD FADVKTIMSN QGSALMGIGV SSGENRAVEA
AKKAISSPLL ETSIVGAQGV LMNITGGESL SLFEAQEAAD IVQDAADEDV NMIFGTVINP
ELQDEIVVTV IATGFDDKPT SHGRKSGSTG FGTSVNTSSN ATSKDESFTS NSSNAQATDS
VSERTHTTKE DDIPSFIRNR EERRSRRTRR
