FTSZ_MYCPU
ID FTSZ_MYCPU Reviewed; 390 AA.
AC Q50318;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=MYPU_4910;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KD735-16;
RX PubMed=8636032; DOI=10.1128/jb.178.8.2314-2319.1996;
RA Wang X., Lutkenhaus J.;
RT "Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism
RT lacking a cell wall.";
RL J. Bacteriol. 178:2314-2319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; U34931; AAC44093.1; -; Genomic_DNA.
DR EMBL; AL445564; CAC13664.1; -; Genomic_DNA.
DR PIR; C90573; C90573.
DR PIR; JC6014; JC6014.
DR RefSeq; WP_010925292.1; NC_002771.1.
DR AlphaFoldDB; Q50318; -.
DR SMR; Q50318; -.
DR STRING; 272635.MYPU_4910; -.
DR EnsemblBacteria; CAC13664; CAC13664; CAC13664.
DR KEGG; mpu:MYPU_4910; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_14; -.
DR OMA; IMNQGGV; -.
DR OrthoDB; 1009041at2; -.
DR BioCyc; MPUL272635:G1GT6-495-MON; -.
DR Proteomes; UP000000528; 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; 3.30.1330.20; -; 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; 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 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..390
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114362"
FT BINDING 20..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 106..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 8
FT /note="V -> I (in Ref. 1; AAC44093)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="I -> T (in Ref. 1; AAC44093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 41508 MW; 2F3B9129B09726D9 CRC64;
MSDLENFVPT ANIKVIGVGG GGNNSVETMI QAGIQGVEFI VANTDIQALQ RSSAPNFIHL
GENKRGLGAG ANPEVGKKAA EESIVEIKEK LKGADMVIIT SGMGGGTGTG ASPIIAKIAR
ELGALTISIV TTPFEFEGNL RNKNAQEGIK NLRAVSDSII IISNNKLLEQ YGDAPMKDSF
LFADTILKHT VKTITDIIAI PAHINLDFAD VKTVMKDKGD ALIGIGRASG KDRAVKAAIH
AISSPIIETS IQGASHTIIN ITGSANLTLT EVHSAVNVIK NAVGPEMNTI FGATINESIG
DEIYVSVIAT GLSSSKKFNS EQEIKDEVSS MLKTMEIDLQ ASETKTILIN DPLPKDEKMV
LTSLLDRDSK ILEKDDSQDD TLPFFLKRNV
