FTSZ_BORBU
ID FTSZ_BORBU Reviewed; 399 AA.
AC P45483; Q59183;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
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=BB_0299;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RA Ge Y., Old I.G., Saint-Girons I., Charon N.W.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-115.
RC STRAIN=212;
RX PubMed=1490605; DOI=10.1016/0378-1097(92)90034-l;
RA Old I.G., Macdougall J.H., Saint-Girons I., Davidson B.E.;
RT "Mapping of genes on the linear chromosome of the bacterium Borrelia
RT burgdorferi: possible locations for its origin of replication.";
RL FEMS Microbiol. Lett. 78:245-250(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC STRAIN=212;
RA Old I.G.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA65464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA78156.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43739; AAA85622.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE000783; AAC66649.2; -; Genomic_DNA.
DR EMBL; X96685; CAA65464.1; ALT_INIT; Genomic_DNA.
DR EMBL; L76303; AAB51402.1; -; Genomic_DNA.
DR EMBL; Z12164; CAA78156.1; ALT_INIT; Genomic_DNA.
DR PIR; C70137; C70137.
DR RefSeq; NP_212433.2; NC_001318.1.
DR RefSeq; WP_002656388.1; NC_001318.1.
DR AlphaFoldDB; P45483; -.
DR SMR; P45483; -.
DR STRING; 224326.BB_0299; -.
DR PRIDE; P45483; -.
DR EnsemblBacteria; AAC66649; AAC66649; BB_0299.
DR KEGG; bbu:BB_0299; -.
DR PATRIC; fig|224326.49.peg.698; -.
DR HOGENOM; CLU_024865_0_1_12; -.
DR OMA; GNPSIGQ; -.
DR Proteomes; UP000001807; 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..399
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114343"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 117..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 115
FT /note="G -> A (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="AA -> RR (in Ref. 3; CAA65464/AAB51402)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="T -> A (in Ref. 3; CAA65464/AAB51402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42398 MW; E808E336343EE583 CRC64;
MKDYNMIDSH TRRFDSTTNP TILKVIGAGG GGSNAVNRMI EYGVRDVEFI VANTDLQALQ
TSIAPIKIAL GAKVTAGLGA GGKPEIGQAA AEEDIDVIRN HLSGADMVFI TAGMGGGTGT
GAAPVIAQVA KELGILTVGV VTKPFKFEGP KKLRLAEQGI NNLRKSVDTL IIIPNQKLLT
VVDKRTTIKD AFKRADDVLR MGVQGIAGLI IEHGEVNIDF ADVKSIMQGQ GDALMGIGYG
KGENRAVDAA TSAISNPLLE EVRIEGSKGL LVNVTGGDDF SLLELEEIMG IITVSVDDEA
TVIYGHAINS NLEDEIYVTV VATGFASKKQ KEISSTPENN TLSSKEFDTL MSGNQNAPSG
SYEQQDSSFA AKSKNVNYFD DDIDVPTFLR NLNKKSSDD
