FTSZ_PSEAE
ID FTSZ_PSEAE Reviewed; 394 AA.
AC P47204;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=PA4407;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8581173; DOI=10.1099/13500872-142-1-79;
RA Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J.,
RA Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.;
RT "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1
RT chromosome.";
RL Microbiology 142:79-86(1996).
RN [2]
RP SEQUENCE REVISION TO 286.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Levesque R.C., Liao X., Lightfoot J., Charlebois I., Ouellet C.,
RA Morency M., Dewar K., Siehnel R., Lam J., Hancock R.E.;
RT "Physical Mapping of 38 loci including aimE, ampC, ampR, arcA, aroK, catR,
RT cypH, dapB, envA, envC, ftsA, ftsZ, groEL, murE, opdE, oprD, oprF, oprH,
RT oprI, oprK, oprP, pbpB, pbpC, pheS, phoA, phoB, phoS, ponA, pyoS1, qin,
RT rpoB, rpoH, sodB, soxR, sucC.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-320 IN COMPLEX WITH SULA AND
RP GDP.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12808143; DOI=10.1073/pnas.1330742100;
RA Cordell S.C., Robinson E.J., Loewe J.;
RT "Crystal structure of the SOS cell division inhibitor SulA and in complex
RT with FtsZ.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7889-7894(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=17900614; DOI=10.1016/j.jmb.2007.08.056;
RA Oliva M.A., Trambaiolo D., Lowe J.;
RT "Structural insights into the conformational variability of FtsZ.";
RL J. Mol. Biol. 373:1229-1242(2007).
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 (By similarity). Interacts directly with
CC several other division proteins (By similarity). Interacts with the
CC SulA inhibitor. {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:12808143}.
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 -!- MISCELLANEOUS: Formation of the FtsZ ring is inhibited by SulA.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; U19797; AAA95993.2; -; Genomic_DNA.
DR EMBL; AE004091; AAG07795.1; -; Genomic_DNA.
DR PIR; H83093; H83093.
DR RefSeq; NP_253097.1; NC_002516.2.
DR RefSeq; WP_003094113.1; NZ_QZGE01000004.1.
DR PDB; 1OFU; X-ray; 2.10 A; A/B=1-320.
DR PDB; 2VAW; X-ray; 2.90 A; A=1-394.
DR PDBsum; 1OFU; -.
DR PDBsum; 2VAW; -.
DR AlphaFoldDB; P47204; -.
DR SMR; P47204; -.
DR IntAct; P47204; 1.
DR STRING; 287.DR97_1585; -.
DR BindingDB; P47204; -.
DR ChEMBL; CHEMBL1075206; -.
DR PaxDb; P47204; -.
DR PRIDE; P47204; -.
DR EnsemblBacteria; AAG07795; AAG07795; PA4407.
DR GeneID; 881296; -.
DR KEGG; pae:PA4407; -.
DR PATRIC; fig|208964.12.peg.4616; -.
DR PseudoCAP; PA4407; -.
DR HOGENOM; CLU_024865_0_1_6; -.
DR InParanoid; P47204; -.
DR OMA; GNPSIGQ; -.
DR PhylomeDB; P47204; -.
DR BioCyc; PAER208964:G1FZ6-4494-MON; -.
DR EvolutionaryTrace; P47204; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..394
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114371"
FT BINDING 21..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:12808143, ECO:0000269|PubMed:17900614"
FT BINDING 108..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:12808143, ECO:0000269|PubMed:17900614"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:12808143, ECO:0000269|PubMed:17900614"
FT BINDING 143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:12808143, ECO:0000269|PubMed:17900614"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:12808143, ECO:0000269|PubMed:17900614"
FT TURN 7..11
FT /evidence="ECO:0007829|PDB:2VAW"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2VAW"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:1OFU"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:2VAW"
FT STRAND 222..233
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:1OFU"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:1OFU"
FT STRAND 305..315
FT /evidence="ECO:0007829|PDB:1OFU"
SQ SEQUENCE 394 AA; 41218 MW; 16ABF06FAB82710F CRC64;
MFELVDNIAQ TAVIKVIGVG GGGGNAVNHM AKNNVEGVEF ICANTDAQAL KNIAARTVLQ
LGPGVTKGLG AGANPEVGRQ AALEDRERIS EVLEGADMVF ITTGMGGGTG TGAAPIIAEV
AKEMGILTVA VVTRPFPFEG RKRMQIADEG IRALAESVDS LITIPNEKLL TILGKDASLL
AAFAKADDVL AGAVRGISDI IKRPGMINVD FADVKTVMSE MGMAMMGTGC ASGPNRAREA
TEAAIRNPLL EDVNLQGARG ILVNITAGPD LSLGEYSDVG NIIEQFASEH ATVKVGTVID
ADMRDELHVT VVATGLGARL EKPVKVVDNT VQGSAAQAAA PAQREQQSVN YRDLDRPTVM
RNQSHGSAAT AAKLNPQDDL DYLDIPAFLR RQAD
