FTSZ_NOSS1
ID FTSZ_NOSS1 Reviewed; 428 AA.
AC P45482;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=alr3858;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8525061; DOI=10.1016/0923-2508(96)80290-7;
RA Zhang C.C., Huguenin S., Friry A.;
RT "Analysis of genes encoding the cell division protein FtsZ and a
RT glutathione synthetase homologue in the cyanobacterium Anabaena sp. PCC
RT 7120.";
RL Res. Microbiol. 146:445-455(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-428.
RX PubMed=7557485; DOI=10.1016/0378-1119(95)00416-4;
RA Doherty H.M., Adams D.G.;
RT "Cloning and sequence of ftsZ and flanking regions from the cyanobacterium
RT Anabaena PCC 7120.";
RL Gene 163:93-96(1995).
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; Z31371; CAA83241.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75557.1; -; Genomic_DNA.
DR EMBL; U14408; AAA85526.1; -; Genomic_DNA.
DR PIR; AC2288; AC2288.
DR PIR; JC4289; JC4289.
DR RefSeq; WP_010997999.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; P45482; -.
DR SMR; P45482; -.
DR STRING; 103690.17132992; -.
DR EnsemblBacteria; BAB75557; BAB75557; BAB75557.
DR KEGG; ana:alr3858; -.
DR eggNOG; COG0206; Bacteria.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR Proteomes; UP000002483; 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..428
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114337"
FT REGION 378..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 386
FT /note="S -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 44730 MW; 853642CA7ACB53D3 CRC64;
MTLDNNQELT YRNSQSLGQP GFSLAVNSSN PFNHSGLNFG QNNDSKKISV ENNRIGEIVP
GRVANIKVIG VGGGGGNAVN RMIESDVSGV EFWSINTDAQ ALTLAGAPSR LQIGQKLTRG
LGAGGNPAIG QKAAEESRDE IATALEGADL VFITAGMGGG TGTGAAPIVA EVAKEMGALT
VGVVTRPFVF EGRRRTSQAE QGIEGLKSRV DTLIIIPNNK LLEVIPEQTP VQEAFRYADD
VLRQGVQGIS DIITIPGLVN VDFADVRAVM ADAGSALMGI GVSSGKSRAR EAAIAAISSP
LLECSIEGAR GVVFNITGGS DLTLHEVNAA AETIYEVVDP NANIIFGAVI DDRLQGEVRI
TVIATGFTGE IQAAPQQNAA NARVVSAPPK RTPTQTPLTN SPAPTPEPKE KSGLDIPDFL
QRRRPPKN
