ID   FTSZ2_PYRFU             Reviewed;         408 AA.
AC   Q8U3E3;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909};
GN   Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=PF0525;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL80649.1; -; Genomic_DNA.
DR   RefSeq; WP_011011642.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U3E3; -.
DR   SMR; Q8U3E3; -.
DR   STRING; 186497.PF0525; -.
DR   PRIDE; Q8U3E3; -.
DR   EnsemblBacteria; AAL80649; AAL80649; PF0525.
DR   GeneID; 41712327; -.
DR   KEGG; pfu:PF0525; -.
DR   PATRIC; fig|186497.12.peg.549; -.
DR   eggNOG; arCOG02201; Archaea.
DR   HOGENOM; CLU_024865_0_1_2; -.
DR   OMA; RAMVIMT; -.
DR   OrthoDB; 41117at2157; -.
DR   PhylomeDB; Q8U3E3; -.
DR   Proteomes; UP000001013; 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..408
FT                   /note="Cell division protein FtsZ 2"
FT                   /id="PRO_0000114410"
FT   BINDING         130..132
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         169
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   408 AA;  44081 MW;  613C1EE19BFA7545 CRC64;
     MLEKLLEQAG IKLDFDGEEE KKSEIVDEFS GYKINIAVVG VGGSGNNTIS RLYDLGVQGA
     DLIAMNTDAQ HLAITKAHKK VLLGKHITQG KGSGGDPKVG YLAAEASAQE IAAAVDGYDL
     VFITAGMGNG TGTGAAPVVA RIVKETARNN GRFQEPLVVS VVTFPFKTEG TVRIEKAKWG
     IQRLLEYSDT VIIIQNDKLL ELVPKLPLQS AFRFADELIA RMVKGIVETI KLNSIVNIDF
     ADVYSIMKGG GPALIGIGES DSNNRAVDAV NNALTNKMLD VEFGSGEKAL VHFTIGPDVS
     LEEINKAMEV VYEKLSEKSE IKWGAMVDPE MGKTVRAMVI MTGVRSPYIL GNVNALTDSS
     SWVVPKDRRL IGDPRIEKMF PDFNGSRAGR KRPSVGDAIL KELGFKEL