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Database: UniProt
Entry: A0A1H0RDT8_9CLOT
LinkDB: A0A1H0RDT8_9CLOT
Original site: A0A1H0RDT8_9CLOT 
ID   A0A1H0RDT8_9CLOT        Unreviewed;       375 AA.
AC   A0A1H0RDT8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631};
GN   Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN   ORFNames=SAMN04488529_103146 {ECO:0000313|EMBL:SDP27704.1};
OS   Clostridium gasigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP27704.1, ECO:0000313|Proteomes:UP000198597};
RN   [1] {ECO:0000313|EMBL:SDP27704.1, ECO:0000313|Proteomes:UP000198597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP27704.1,
RC   ECO:0000313|Proteomes:UP000198597};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000631}.
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:RU000631}.
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DR   EMBL; FNJM01000003; SDP27704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0RDT8; -.
DR   STRING; 94869.SAMN04488529_103146; -.
DR   OrthoDB; 9813375at2; -.
DR   Proteomes; UP000198597; Unassembled WGS sequence.
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; Tubulin/FtsZ, C-terminal domain; 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; 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   NCBIfam; TIGR00065; ftsZ; 1.
DR   PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR   PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 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:RU000631};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
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:UP000198597};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          13..205
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          207..324
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   BINDING         21..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         108..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   375 AA;  39940 MW;  527A93E923D4D55C CRC64;
     MLDFEVDMQE LTNIKVVGCG GGGGNAVNRM ITEGLKNVEF IVVNTDKQAL MLSHANIKIQ
     IGEKLTKGLG AGANPEIGKK AAEESREEIA ESIKGANMVF ITAGMGGGTG TGAAPIVAQI
     AKSMNILTVG VVTKPFPFEG KRRMTHAEMG IENLMQAVDT LVIIPNHRLL LMADKKTTLL
     DSFRLADDVL RQGVQAISDL ITIPGVVNAD FADIETVMLN KGLAHMGVGY GTGDNKAQDA
     VRQAISSPLL ETSIDGATGV IINFTGGVDL GAIEVFEAAD IVRESADPDA NIIFGAVIDE
     TLNDEIRITV IATGFEEDEN KVPQAKPVVE TKRFSGKANN VVAEEPVIQE MPKADPLLEF
     DTESVNIPSF LRTRK
//
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