FTSZ_CAUVN
ID FTSZ_CAUVN Reviewed; 508 AA.
AC B8H080; P52976;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=CCNA_02623;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8692812; DOI=10.1073/pnas.93.13.6314;
RA Quardokus E., Din N., Brun Y.V.;
RT "Cell cycle regulation and cell type-specific localization of the FtsZ
RT division initiation protein in Caulobacter.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6314-6319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; U40273; AAC44223.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL96088.1; -; Genomic_DNA.
DR RefSeq; WP_010920397.1; NC_011916.1.
DR RefSeq; YP_002517996.1; NC_011916.1.
DR AlphaFoldDB; B8H080; -.
DR SMR; B8H080; -.
DR IntAct; B8H080; 1.
DR PRIDE; B8H080; -.
DR EnsemblBacteria; ACL96088; ACL96088; CCNA_02623.
DR GeneID; 7332973; -.
DR KEGG; ccs:CCNA_02623; -.
DR PATRIC; fig|565050.3.peg.2572; -.
DR HOGENOM; CLU_024865_5_2_5; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR PhylomeDB; B8H080; -.
DR Proteomes; UP000001364; 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..508
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000378290"
FT REGION 342..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 236
FT /note="G -> A (in Ref. 1; AAC44223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 54207 MW; 4E817C099F58C4CE CRC64;
MAISLSAPRT TELKPRIVVF GVGGAGGNAV NNMIEAGLEG VEFVVANTDA QQLQFAKTDR
RIQLGVQITQ GLGAGAHPEV GMSAAEESFP EIGEHLDGAH MVFITAGMGG GTGTGAAPII
AKCARERGIL TVGVVTKPFH FEGRHRMRLA DSGIQELQRY VDTLIVIPNQ NLFRVANERT
TFAEAFGMAD QVLHSGVRSI TDLMVLPGLI NLDFADVRTV MTEMGKAMMG TGEGTGEDRA
LMAAQNAIAN PLLDEVSLKG AKAVLVNVTG GMDMTLLEVD EAANAISDQV DPEANIIFGA
AFDPSLEGVI RVSVVATGMD GASIAQIEPK PVSRNISAAP LIAETSRPAP QPEPARPTAR
YEAARPAERP VAFAPEPAPE PEIVMSAPQP EPEAELYYDE PTVAEEPRVS AAPARSVNRI
VDPLVDDVAE EPLFPENNYY EERRPQKQGG FFSMFGGGRQ RYEQQASAPQ AQARSAQSAR
PQLQPIETPQ ADDAEDLEIP SFLRRLAN
