FTSZ2_HALS3
ID FTSZ2_HALS3 Reviewed; 393 AA.
AC B0R2V3; Q48290; Q9HSK0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=OE_1319R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=R1 / S9 / Pho81;
RX PubMed=8631708; DOI=10.1128/jb.178.5.1320-1327.1996;
RA Margolin W., Wang R., Kumar M.;
RT "Isolation of an ftsZ homolog from the archaebacterium Halobacterium
RT salinarium: implications for the evolution of FtsZ and tubulin.";
RL J. Bacteriol. 178:1320-1327(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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. Overexpression
CC causes significant changes in cell morphology (PubMed:8631708).
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:8631708}.
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=AAB06191.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM774415; CAP13063.1; -; Genomic_DNA.
DR EMBL; U32860; AAB06191.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012289116.1; NC_010364.1.
DR AlphaFoldDB; B0R2V3; -.
DR SMR; B0R2V3; -.
DR EnsemblBacteria; CAP13063; CAP13063; OE_1319R.
DR GeneID; 5952416; -.
DR GeneID; 62885920; -.
DR KEGG; hsl:OE_1319R; -.
DR HOGENOM; CLU_024865_0_1_2; -.
DR OMA; IMNQGGV; -.
DR PhylomeDB; B0R2V3; -.
DR Proteomes; UP000001321; 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 Septation.
FT CHAIN 1..393
FT /note="Cell division protein FtsZ 2"
FT /id="PRO_0000414241"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 127..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ SEQUENCE 393 AA; 41318 MW; 5C482EC36D0000EA CRC64;
MQDIVQDALD NAEAEQREMD GDGDGDEFGD PRIVIVGCGG AGNNTVNRLY NIGVEGADTV
AINTDKQHLK MIKADTKILV GKSLTNGLGA GGDPSMGERA TEMAQGTIKE VLGDADLVFV
TAGMGGGTGT GAAPVVSKIA KEQGAIVVGM VSTPFNVERA RTVKAEEGLE KLREKADSII
VLDNNRLLDY VPNLPIGKAF SVMDQIIAET VKGISETITQ PSLINLDYAD MTAIMNQGGV
AVMLVGETQD KNKTNEVVKD AMNHPLLDVD YRGASGGLVH ITGGPDLTLK EAEGIADNIT
ERLDASANVI WGARIQESYK GKVRVMAIMT GVQSAQVLGP STQKQADKSR RELQDVDSKQ
RAADDAGAGG FGGAHSDGGQ DEVEQENGLD VIR
