ID   FTSZ_MYCPN              Reviewed;         380 AA.
AC   P75464;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN   Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=MPN_317;
GN   ORFNames=MP519;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96167.1; -; Genomic_DNA.
DR   PIR; S73845; S73845.
DR   RefSeq; NP_110005.1; NC_000912.1.
DR   RefSeq; WP_010874673.1; NC_000912.1.
DR   AlphaFoldDB; P75464; -.
DR   SMR; P75464; -.
DR   IntAct; P75464; 4.
DR   STRING; 272634.MPN_317; -.
DR   PRIDE; P75464; -.
DR   EnsemblBacteria; AAB96167; AAB96167; MPN_317.
DR   KEGG; mpn:MPN_317; -.
DR   PATRIC; fig|272634.6.peg.340; -.
DR   HOGENOM; CLU_024865_1_1_14; -.
DR   OMA; ASENIHF; -.
DR   BioCyc; MPNE272634:G1GJ3-507-MON; -.
DR   Proteomes; UP000000808; 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; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR30314; PTHR30314; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; SSF52490; 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..380
FT                   /note="Cell division protein FtsZ"
FT                   /id="PRO_0000114361"
FT   BINDING         27..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         119..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   380 AA;  42797 MW;  6C3B531C63F4997E CRC64;
     MDWIQTAGAG TQLPENNIKI AVFGIGGAGN NIIDDMLRMH PELQTANVQF FALNTDLQHL
     KTKRYVQNKA VIQFEESKGL GVGGDPQKGA VLAHHFLEQF HKLSDSFDFC ILVAGFGKGT
     GTGATPVFSK FLSNKGVLNL SIVSYPAMCE GLKAREKAAK GLERLNQATD SFMLFRNDRC
     TDGIYQLANV AIVKTIKNII ELINLPLQQN IDFEDIRSFF KKPAQRLENE ANLFRVTNTF
     TFSFDAHNTI EHFSHKLKNF EYEGFFDHKV EGAQKVILKV LVNQGLYPLD LTQIQEIIWA
     KIDNHNLEVQ LGVDFTDANP SVQLFFLMEK KQAVSSDFIQ KPAFISVKEV NQKPAKPFQV
     LNDLKELGLK YVKQQTGFNY