FTSZ1_METJA
ID FTSZ1_METJA Reviewed; 364 AA.
AC Q57816;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cell division protein FtsZ 1 {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ1 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=MJ0370;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=9428770; DOI=10.1038/34472;
RA Loewe J., Amos L.A.;
RT "Crystal structure of the bacterial cell-division protein ftsZ.";
RL Nature 391:203-206(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-356.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=10049809; DOI=10.1006/jsbi.1998.4041;
RA Loewe J.;
RT "Crystal structure determination of FtsZ from Methanococcus jannaschii.";
RL J. Struct. Biol. 124:235-243(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GTP, AND SUBUNIT.
RX PubMed=15558053; DOI=10.1038/nsmb855;
RA Oliva M.A., Cordell S.C., Lowe J.;
RT "Structural insights into FtsZ protofilament formation.";
RL Nat. Struct. Mol. Biol. 11:1243-1250(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 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 (PubMed:15558053). Polymerizes to form a dynamic
CC ring structure in a strictly GTP-dependent manner. Interacts directly
CC with several other division proteins (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:15558053}.
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; L77117; AAB98359.1; -; Genomic_DNA.
DR PIR; B64346; B64346.
DR RefSeq; WP_010869869.1; NC_000909.1.
DR PDB; 1FSZ; X-ray; 2.80 A; A=1-364.
DR PDB; 1W58; X-ray; 2.50 A; 1=1-364.
DR PDB; 1W59; X-ray; 2.70 A; A/B=1-364.
DR PDB; 1W5A; X-ray; 2.40 A; A/B=1-364.
DR PDB; 1W5B; X-ray; 2.20 A; A/B=1-364.
DR PDB; 1W5E; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-364.
DR PDB; 2VAP; X-ray; 1.70 A; A=1-364.
DR PDBsum; 1FSZ; -.
DR PDBsum; 1W58; -.
DR PDBsum; 1W59; -.
DR PDBsum; 1W5A; -.
DR PDBsum; 1W5B; -.
DR PDBsum; 1W5E; -.
DR PDBsum; 2VAP; -.
DR AlphaFoldDB; Q57816; -.
DR SMR; Q57816; -.
DR STRING; 243232.MJ_0370; -.
DR EnsemblBacteria; AAB98359; AAB98359; MJ_0370.
DR GeneID; 1451227; -.
DR KEGG; mja:MJ_0370; -.
DR eggNOG; arCOG02201; Archaea.
DR HOGENOM; CLU_024865_0_1_2; -.
DR InParanoid; Q57816; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 41117at2157; -.
DR PhylomeDB; Q57816; -.
DR BRENDA; 3.6.5.6; 3260.
DR EvolutionaryTrace; Q57816; -.
DR Proteomes; UP000000805; 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..364
FT /note="Cell division protein FtsZ 1"
FT /id="PRO_0000114401"
FT BINDING 47..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15558053,
FT ECO:0000269|PubMed:17900614, ECO:0000269|PubMed:9428770"
FT BINDING 97..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15558053"
FT BINDING 134..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15558053, ECO:0000269|PubMed:17900614,
FT ECO:0000269|PubMed:9428770"
FT BINDING 165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15558053, ECO:0000269|PubMed:17900614,
FT ECO:0000269|PubMed:9428770"
FT BINDING 169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15558053, ECO:0000269|PubMed:9428770"
FT BINDING 212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|PubMed:15558053, ECO:0000269|PubMed:17900614,
FT ECO:0000269|PubMed:9428770"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:1W59"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2VAP"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1W59"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1W58"
FT HELIX 204..227
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1W58"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:2VAP"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:1W5B"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:2VAP"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2VAP"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:2VAP"
SQ SEQUENCE 364 AA; 38924 MW; 3BB386A5D2FCA107 CRC64;
MKFLKNVLEE GSKLEEFNEL ELSPEDKELL EYLQQTKAKI TVVGCGGAGN NTITRLKMEG
IEGAKTVAIN TDAQQLIRTK ADKKILIGKK LTRGLGAGGN PKIGEEAAKE SAEEIKAAIQ
DSDMVFITCG LGGGTGTGSA PVVAEISKKI GALTVAVVTL PFVMEGKVRM KNAMEGLERL
KQHTDTLVVI PNEKLFEIVP NMPLKLAFKV ADEVLINAVK GLVELITKDG LINVDFADVK
AVMNNGGLAM IGIGESDSEK RAKEAVSMAL NSPLLDVDID GATGALIHVM GPEDLTLEEA
REVVATVSSR LDPNATIIWG ATIDENLENT VRVLLVITGV QSRIEFTDTG LKRKKLELTG
IPKI
