FTSZ_STAAM
ID FTSZ_STAAM Reviewed; 390 AA.
AC P0A029; P45498;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=SAV1186;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 12-316 OF APOPROTEIN AND IN
RP COMPLEXES WITH GDP AND INHIBITOR, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ASN-208.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=22948918; DOI=10.1107/s0907444912022640;
RA Matsui T., Yamane J., Mogi N., Yamaguchi H., Takemoto H., Yao M.,
RA Tanaka I.;
RT "Structural reorganization of the bacterial cell-division protein FtsZ from
RT Staphylococcus aureus.";
RL Acta Crystallogr. D 68:1175-1188(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF WILD-TYPE AND OF MUTANTS IN
RP COMPLEXES WITH GTP AND GDP.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=24347164; DOI=10.1074/jbc.m113.514901;
RA Matsui T., Han X., Yu J., Yao M., Tanaka I.;
RT "Structural change in FtsZ induced by intermolecular interactions between
RT bound GTP and the T7 loop.";
RL J. Biol. Chem. 289:3501-3509(2014).
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 -!- ACTIVITY REGULATION: Calcium ions inhibit the GTPase activity and
CC promote the polymerization of FtsZ. {ECO:0000269|PubMed:22948918}.
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; BA000017; BAB57348.1; -; Genomic_DNA.
DR RefSeq; WP_000888997.1; NC_002758.2.
DR PDB; 3VO8; X-ray; 2.26 A; A/B=1-390.
DR PDB; 3VO9; X-ray; 2.71 A; A/B/C/D=12-316.
DR PDB; 3VOA; X-ray; 1.73 A; A=12-316.
DR PDB; 3VOB; X-ray; 2.70 A; A=12-316.
DR PDB; 3VPA; X-ray; 2.49 A; A/B/C/D=12-316.
DR PDB; 3WGJ; X-ray; 2.18 A; A/B=12-316.
DR PDB; 3WGK; X-ray; 2.80 A; A/B=1-390.
DR PDB; 3WGL; X-ray; 3.07 A; A/B=1-390.
DR PDB; 3WGM; X-ray; 2.09 A; A/B=1-390.
DR PDB; 3WGN; X-ray; 2.61 A; A/B=1-390.
DR PDBsum; 3VO8; -.
DR PDBsum; 3VO9; -.
DR PDBsum; 3VOA; -.
DR PDBsum; 3VOB; -.
DR PDBsum; 3VPA; -.
DR PDBsum; 3WGJ; -.
DR PDBsum; 3WGK; -.
DR PDBsum; 3WGL; -.
DR PDBsum; 3WGM; -.
DR PDBsum; 3WGN; -.
DR AlphaFoldDB; P0A029; -.
DR SMR; P0A029; -.
DR World-2DPAGE; 0002:P0A029; -.
DR PaxDb; P0A029; -.
DR EnsemblBacteria; BAB57348; BAB57348; SAV1186.
DR KEGG; sav:SAV1186; -.
DR HOGENOM; CLU_024865_0_1_9; -.
DR OMA; GNPSIGQ; -.
DR PhylomeDB; P0A029; -.
DR BioCyc; SAUR158878:SAV_RS06405-MON; -.
DR Proteomes; UP000002481; 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; 3.30.1330.20; -; 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_0000114380"
FT REGION 315..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..380
FT /note="Interaction with FtsA"
FT /evidence="ECO:0000250"
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 ECO:0000269|PubMed:22948918, ECO:0000269|PubMed:24347164"
FT BINDING 29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22948918,
FT ECO:0000269|PubMed:24347164"
FT BINDING 71..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24347164"
FT BINDING 108..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:22948918, ECO:0000269|PubMed:24347164"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:22948918, ECO:0000269|PubMed:24347164"
FT BINDING 143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:22948918, ECO:0000269|PubMed:24347164"
FT BINDING 166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22948918,
FT ECO:0000269|PubMed:24347164"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:24347164"
FT MUTAGEN 208
FT /note="N->A: Lack of GTPase activity. Does not polymerize
FT in the presence of calcium ions."
FT /evidence="ECO:0000269|PubMed:22948918"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:3VPA"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:3VOA"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:3VOA"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3WGM"
FT STRAND 303..313
FT /evidence="ECO:0007829|PDB:3VOA"
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
