ID N0BNG7_9EURY Unreviewed; 388 AA.
AC N0BNG7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU003360};
GN Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN ORFNames=Asulf_01894 {ECO:0000313|EMBL:AGK61860.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK61860.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK61860.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK61860.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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:0000256|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:0000256|HAMAP-Rule:MF_00909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane. {ECO:0000256|HAMAP-Rule:MF_00909}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|ARBA:ARBA00009690,
CC ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU003360}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00909}.
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DR EMBL; CP005290; AGK61860.1; -; Genomic_DNA.
DR RefSeq; WP_015591456.1; NC_021169.1.
DR AlphaFoldDB; N0BNG7; -.
DR STRING; 387631.Asulf_01894; -.
DR GeneID; 15393528; -.
DR KEGG; ast:Asulf_01894; -.
DR eggNOG; arCOG02201; Archaea.
DR HOGENOM; CLU_024865_0_1_2; -.
DR OrthoDB; 371908at2157; -.
DR Proteomes; UP000013307; 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; Tubulin/FtsZ, GTPase domain; 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 NCBIfam; TIGR00065; ftsZ; 1.
DR PANTHER; PTHR30314:SF9; CELL DIVISION PROTEIN FTSZ 2; 1.
DR PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909,
KW ECO:0000256|RuleBase:RU003360};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW ECO:0000256|RuleBase:RU003360};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00909};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00909}; Reference proteome {ECO:0000313|Proteomes:UP000013307};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00909}.
FT DOMAIN 33..223
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 225..342
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT BINDING 128..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ SEQUENCE 388 AA; 42390 MW; FA8A67FA168C2962 CRC64;
MKSLVSEAQK YYMEERNRRM SSNFDIEEYG LPKIIVVGCG GSGNNTITRL KQLGVEGVTT
IAINTDKQHL LNTQADKRVL IGRTLTKGLG AGGYPEIGRK AAELARGTLE ELLSGADLVF
VCAGMGGGTG TGSAPVVAEI AKKQGAIVIG MVQTPFRVER ARIKKAEEGL EELRKQADTV
VVLDNNKLLE YVPNLPIEQA FSVMDQLISE TIKGISDTIT QPSLMNIDFA DVRAVMGQGG
VAVMLVGESR SQNKAKDVVK DCLNHPLLEV DYRGAKGALI HLSGGTDLTI KEAEEIVNNL
TFEIDDAANV IWGARISKEM EGCVRVMAIM TGVSSPNIIS RNLIEEEANF ENGNGRSKFR
KIEKIQRAKK LEKVVRSRRS YLREIDRL
//
