FTSZ_THEAC
ID FTSZ_THEAC Reviewed; 395 AA.
AC O59635;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=Ta0072;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10973825; DOI=10.1006/bbrc.2000.3401;
RA Yaoi T., Laksanalamai P., Jiemjit A., Kagawa H., Alton T., Trent J.D.;
RT "Cloning and characterization of ftsZ and pyrF from the archaeon
RT Thermoplasma acidophilum.";
RL Biochem. Biophys. Res. Commun. 275:936-945(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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. {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; AF038845; AAC24043.1; -; Genomic_DNA.
DR EMBL; AL445063; CAC11220.1; -; Genomic_DNA.
DR PIR; T37331; T37331.
DR RefSeq; WP_010900500.1; NC_002578.1.
DR AlphaFoldDB; O59635; -.
DR SMR; O59635; -.
DR STRING; 273075.Ta0072; -.
DR EnsemblBacteria; CAC11220; CAC11220; CAC11220.
DR GeneID; 1455732; -.
DR KEGG; tac:Ta0072; -.
DR eggNOG; arCOG02201; Archaea.
DR HOGENOM; CLU_024865_0_1_2; -.
DR OrthoDB; 41117at2157; -.
DR Proteomes; UP000001024; 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; 3.40.50.1440; -; 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; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Septation.
FT CHAIN 1..395
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114417"
FT BINDING 52..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 139..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 199
FT /note="K -> R (in Ref. 2; CAC11220)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..395
FT /note="AGEHVHRIICGRDRHGELDQPMIRENIFFNLIITT -> LASMFTGSYAAEI
FT DTVN (in Ref. 2; CAC11220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 42526 MW; 9211322158445E10 CRC64;
MGDITDLLSK VSIDDVYDEW EDQASGSLPE DAEIENVYKT LNVKIKVIGC GGGGSNTVNR
LYDDALKNAD LIAINTDASH LRSIKVKHKL LIGQKTTKGL GTGADPKVGE EAAIEEIVAI
KKIVQNTDIT FVTAGLGGGT GTGCAPVIAR AAKEAGSIVI SVVTLPFESE GPLRMDNAVI
GLEKLAQFSD TLVAIPNQKL LSEVPNAEMK VAFAYADKVL ADTIRSIVEI ITKTGIINID
YSDIKTVMQS GGVALIGMGQ SKKGGDRIMT ALEEALKPRL IDVDVSTAKD CVFKIIAPPD
ITVSEVGKAM DEIKKKINPR SRIIWGLTID KDLDKDVKVL IFMTGVSSAY LVKDVESARK
AGEHVHRIIC GRDRHGELDQ PMIRENIFFN LIITT
