FTSZ_PORGI
ID FTSZ_PORGI Reviewed; 457 AA.
AC O08466;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, 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=PG_0584;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=381;
RA Akifusa S., Tamura H., Ansai T., Takehara T.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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; AB004555; BAA28179.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65771.1; -; Genomic_DNA.
DR RefSeq; WP_005873941.1; NC_002950.2.
DR AlphaFoldDB; O08466; -.
DR SMR; O08466; -.
DR STRING; 242619.PG_0584; -.
DR EnsemblBacteria; AAQ65771; AAQ65771; PG_0584.
DR KEGG; pgi:PG_0584; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_10; -.
DR OMA; IMNQGGV; -.
DR OrthoDB; 1009041at2; -.
DR Proteomes; UP000000588; 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; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_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; 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..457
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114370"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 115..117
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 150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 52
FT /note="V -> L (in Ref. 1; BAA28179)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> P (in Ref. 1; BAA28179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50261 MW; A1BEB31F693CD08A CRC64;
MEDELLNFNY TDSGLPVIIK VIGVGGGGGN AVKNMYHGKV RDVSFLLCNT DVQALDRSEV
PDRLVLGREV TNGLGAGSRP EVARRAAEAS EADIRKILDD GHTRMVFVTA GMGGGTGTGA
APVIGRIARE LNILTVGIVT IPFVFEGKRK ILQALEGVEE MRKNVDALLV VNNERLRIIY
KDLKLDNAFA KADETLTNAA NGIAEMIMKE GTINLDFADV HTTLKDGGIA IISTGYGEGP
DRMEQAINEA LTSPLLNNND IFKARRVLFN IYQGTEDPLG TDELSAINEL TAKIETGFDT
IWGYTTDPEL GKKVKITILA SGFDLDTTRE SIRIGDNLGN VINDPISSRE IETQNERDND
LINRYYRPDE LEKVKVVDFK PIILNLDELD NDELIMALEE KPAYSRTGVL LSRIDNIRMR
IAESAGRLKK DVVRSEESER PAFESERSSS PTTISFN
