FTSZ_STAAU
ID FTSZ_STAAU Reviewed; 390 AA.
AC P0A031; P45498;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SA4;
RA Alessi D.M., Olson E.R.;
RT "Cloning and sequencing of an ftsZ homologue from Staphylococcus aureus.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH FTSA, SELF-INTERACTION, AND MUTAGENESIS OF ASP-371;
RP ASP-372; ILE-373; PRO-374; SER-375; PHE-376; ILE-377; ARG-378; ASN-379 AND
RP ARG-380.
RC STRAIN=WCUH29 / NCIMB 40771;
RX PubMed=10753635; DOI=10.1006/bbrc.2000.2439;
RA Yan K., Pearce K.H., Payne D.J.;
RT "A conserved residue at the extreme C-terminus of FtsZ is critical for the
RT FtsA-FtsZ interaction in Staphylococcus aureus.";
RL Biochem. Biophys. Res. Commun. 270:387-392(2000).
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 (By similarity). Interacts with FtsA.
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:10753635}.
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}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Becoming two - Issue 171 of
CC July 2015;
CC URL="https://web.expasy.org/spotlight/back_issues/171/";
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DR EMBL; U06462; AAA16512.1; -; Unassigned_DNA.
DR PIR; S58814; S58814.
DR RefSeq; WP_000888997.1; NZ_WYDB01000002.1.
DR PDB; 4DXD; X-ray; 2.01 A; A=2-390.
DR PDB; 5MN4; X-ray; 1.50 A; A=12-316.
DR PDB; 5MN5; X-ray; 2.80 A; A/B=12-316.
DR PDB; 5MN6; X-ray; 3.20 A; A/B=12-316.
DR PDB; 5MN7; X-ray; 3.30 A; A/B=12-316.
DR PDB; 5MN8; X-ray; 3.50 A; A/B=12-316.
DR PDB; 6KVP; X-ray; 1.40 A; A=12-316.
DR PDB; 6KVQ; X-ray; 1.60 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 PDBsum; 4DXD; -.
DR PDBsum; 5MN4; -.
DR PDBsum; 5MN5; -.
DR PDBsum; 5MN6; -.
DR PDBsum; 5MN7; -.
DR PDBsum; 5MN8; -.
DR PDBsum; 6KVP; -.
DR PDBsum; 6KVQ; -.
DR PDBsum; 6YD1; -.
DR PDBsum; 6YD5; -.
DR PDBsum; 6YD6; -.
DR AlphaFoldDB; P0A031; -.
DR SMR; P0A031; -.
DR BindingDB; P0A031; -.
DR ChEMBL; CHEMBL5096; -.
DR OMA; GNPSIGQ; -.
DR PRO; PR:P0A031; -.
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; 3.30.1330.20; -; 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; Septation.
FT CHAIN 1..390
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114385"
FT REGION 315..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..380
FT /note="Interaction with FtsA"
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 MUTAGEN 371
FT /note="D->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 372
FT /note="D->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 373
FT /note="I->P: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 374
FT /note="P->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 375
FT /note="S->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 376
FT /note="F->A: No interaction with FtsA, but does not affect
FT interaction with FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 377
FT /note="I->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 378
FT /note="R->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 379
FT /note="N->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT MUTAGEN 380
FT /note="R->A: Does not affect interaction with FtsA and
FT FtsZ."
FT /evidence="ECO:0000269|PubMed:10753635"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5MN6"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5MN7"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:5MN4"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5MN7"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5MN5"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5MN4"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5MN4"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:5MN4"
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
