ID J5UNZ7_9FIRM Unreviewed; 379 AA.
AC J5UNZ7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:EJU24004.1};
GN ORFNames=HMPREF1152_0991 {ECO:0000313|EMBL:EJU24004.1};
OS Mogibacterium sp. CM50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU24004.1, ECO:0000313|Proteomes:UP000003142};
RN [1] {ECO:0000313|EMBL:EJU24004.1, ECO:0000313|Proteomes:UP000003142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM50 {ECO:0000313|EMBL:EJU24004.1,
RC ECO:0000313|Proteomes:UP000003142};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJU24004.1}.
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DR EMBL; ALNL01000006; EJU24004.1; -; Genomic_DNA.
DR RefSeq; WP_009643144.1; NZ_ALNL01000006.1.
DR AlphaFoldDB; J5UNZ7; -.
DR STRING; 936375.HMPREF1152_0991; -.
DR PATRIC; fig|936375.3.peg.78; -.
DR eggNOG; COG0206; Bacteria.
DR OrthoDB; 9813375at2; -.
DR Proteomes; UP000003142; 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:UP000003142};
KW Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 17..209
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 211..328
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 112..114
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 147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ SEQUENCE 379 AA; 39989 MW; 51074E402CE3A05D CRC64;
MMEFVSDFVS STDNAAIIKV VGVGGGGCNA INRMVDENLQ GVTFIAVNTD KQALAKCKAE
VKIQIGEKLT GGRGAGANPE IGQKAAEETL EEISSYLQDA DMVFVTAGMG GGTGTGAAPI
IAKASMDCGA LTVAVVTKPF SFEGKKRWNR ATKGIQYLTN FVDSLVIIPN DRLIDSSEKN
TTMIEAFSMA DDVLRQGVQG ISDLISEYGI VNVDFADVKT IMEGRGVAHM GVGIGTGDNK
IEDAVRNAIE SPLLETSIDG ARSILLYVCG GYDIGMQDIS KIASKIQDEA DPEANIIFGA
TVNENMNDKV SITLIATDFT TGGLAPAGET PEVARPSVKG TRVNVDGLEG QIVDMSDFMK
DDNQADKGSS DFDVPDFLK
//
