FTSZ_THEMA
ID FTSZ_THEMA Reviewed; 351 AA.
AC O08398;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=TM_0836;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CHARACTERIZATION.
RX PubMed=9605973;
RX DOI=10.1002/(sici)1097-0169(1998)40:1<71::aid-cm7>3.0.co;2-i;
RA Lu C., Stricker J., Erickson H.P.;
RT "FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga
RT maritima -- quantitation, GTP hydrolysis, and assembly.";
RL Cell Motil. Cytoskeleton 40:71-86(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=15558053; DOI=10.1038/nsmb855;
RA Oliva M.A., Cordell S.C., Lowe J.;
RT "Structural insights into FtsZ protofilament formation.";
RL Nat. Struct. Mol. Biol. 11:1243-1250(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 336-351 IN COMPLEX WITH FTSA.
RX PubMed=22473211; DOI=10.1038/emboj.2012.76;
RA Szwedziak P., Wang Q., Freund S.M., Lowe J.;
RT "FtsA forms actin-like protofilaments.";
RL EMBO J. 31:2249-2260(2012).
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:9605973}.
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 (PubMed:22473211). {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:22473211}.
CC -!- INTERACTION:
CC O08398; Q9WZU0: ftsA; NbExp=4; IntAct=EBI-7808310, EBI-7808292;
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; U65944; AAC24604.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35918.1; -; Genomic_DNA.
DR PIR; H72328; H72328.
DR RefSeq; NP_228645.1; NC_000853.1.
DR RefSeq; WP_004080800.1; NZ_CP011107.1.
DR PDB; 1W5F; X-ray; 2.00 A; A/B=1-351.
DR PDB; 4A2A; X-ray; 1.80 A; C/D=336-351.
DR PDBsum; 1W5F; -.
DR PDBsum; 4A2A; -.
DR AlphaFoldDB; O08398; -.
DR SMR; O08398; -.
DR IntAct; O08398; 1.
DR MINT; O08398; -.
DR STRING; 243274.THEMA_00460; -.
DR DrugBank; DB03532; Phosphomethylphosphonic acid guanylate ester.
DR EnsemblBacteria; AAD35918; AAD35918; TM_0836.
DR KEGG; tma:TM0836; -.
DR eggNOG; COG0206; Bacteria.
DR InParanoid; O08398; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR EvolutionaryTrace; O08398; -.
DR Proteomes; UP000008183; 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..351
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114391"
FT BINDING 31..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 118..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 197
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 102
FT /note="V -> A (in Ref. 1; AAC24604)"
FT /evidence="ECO:0000305"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1W5F"
FT TURN 73..78
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:1W5F"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 189..212
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 232..243
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:1W5F"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:1W5F"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4A2A"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4A2A"
SQ SEQUENCE 351 AA; 38307 MW; 5F2E11FDAA92AFE7 CRC64;
MGFDLDVEKK KENRNIPQAN NLKIKVIGVG GAGNNAINRM IEIGIHGVEF VAVNTDLQVL
EASNADVKIQ IGENITRGLG AGGRPEIGEQ AALESEEKIR EVLQDTHMVF ITAGFGGGTG
TGASPVIAKI AKEMGILTVA IVTTPFYFEG PERLKKAIEG LKKLRKHVDT LIKISNNKLM
EELPRDVKIK DAFLKADETL HQGVKGISEL ITKRGYINLD FADIESVMKD AGAAILGIGV
GKGEHRAREA AKKAMESKLI EHPVENASSI VFNITAPSNI RMEEVHEAAM IIRQNSSEDA
DVKFGLIFDD EVPDDEIRVI FIATRFPDED KILFPEGDIP AIYRYGLEGL L
