FTSZ_NEIMB
ID FTSZ_NEIMB Reviewed; 392 AA.
AC P0A0S6; Q51130;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=NMB0427;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NMB / Serogroup B;
RA Ribot E.M., Quinn F.D., Stephens D.S., Raymond N.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; U43329; AAB18147.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40865.1; -; Genomic_DNA.
DR PIR; E81199; E81199.
DR RefSeq; NP_273475.1; NC_003112.2.
DR RefSeq; WP_002212501.1; NC_003112.2.
DR AlphaFoldDB; P0A0S6; -.
DR SMR; P0A0S6; -.
DR STRING; 122586.NMB0427; -.
DR PaxDb; P0A0S6; -.
DR PRIDE; P0A0S6; -.
DR EnsemblBacteria; AAF40865; AAF40865; NMB0427.
DR GeneID; 61281969; -.
DR KEGG; nme:NMB0427; -.
DR PATRIC; fig|122586.8.peg.541; -.
DR HOGENOM; CLU_024865_0_1_4; -.
DR OMA; GNPSIGQ; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
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..392
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114369"
FT BINDING 24..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 111..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 145
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"
FT CONFLICT 30
FT /note="I -> S (in Ref. 1; AAB18147)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..392
FT /note="MIRTNRGIRTMNLTAADFDNQSVLDDFEIPAILRRQHNSDK -> RSAPIAV
FT SAR (in Ref. 1; AAB18147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 41487 MW; 4900B04AF6138221 CRC64;
MEFVYDVAES AVSPAVIKVI GLGGGGCNAI NNMVANNVRG VEFISANTDA QSLAKNHAAK
RIQLGTNLTR GLGAGANPDI GRAAAQEDRE AIEEAIRGAN MLFITTGMGG GTGTGSAPVV
AEIAKSLGIL TVAVVTRPFA YEGKRVHVAQ AGLEQLKEHV DSLIIIPNDK LMTALGEDVT
MREAFRAADN VLRDAVAGIS EVVTCPSEII NLDFADVKTV MSNRGIAMMG SGYAQGIDRA
RMATDQAISS PLLDDVTLDG ARGVLVNITT APGCLKMSEL SEVMKIVNQS AHPDLECKFG
AAEDETMSED AIRITIIATG LKEKGAVDFV PAREVEAVAP SKQEQSHNVE GMIRTNRGIR
TMNLTAADFD NQSVLDDFEI PAILRRQHNS DK
