FTSZ1_HALVD
ID FTSZ1_HALVD Reviewed; 379 AA.
AC Q48327; D4GT76;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cell division protein FtsZ 1 {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ1 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=HVO_0717;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GTPASE, GTP-BINDING,
RP SUBCELLULAR LOCATION, AND RING-LIKE STRUCTURE.
RX PubMed=8858586; DOI=10.1046/j.1365-2958.1996.6421360.x;
RA Wang X., Lutkenhaus J.;
RT "FtsZ ring: the eubacterial division apparatus conserved in
RT archaebacteria.";
RL Mol. Microbiol. 21:313-319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000303|PubMed:34103513};
RX PubMed=34103513; DOI=10.1038/s41467-021-23686-9;
RA Nussbaum P., Gerstner M., Dingethal M., Erb C., Albers S.V.;
RT "The archaeal protein SepF is essential for cell division in Haloferax
RT volcanii.";
RL Nat. Commun. 12:3469-3469(2021).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP ASP-250, AND PHYLOGENETIC ANALYSIS.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000303|PubMed:33903747};
RX PubMed=33903747; DOI=10.1038/s41564-021-00894-z;
RA Liao Y., Ithurbide S., Evenhuis C., Loewe J., Duggin I.G.;
RT "Cell division in the archaeon Haloferax volcanii relies on two FtsZ
RT proteins with distinct functions in division ring assembly and
RT constriction.";
RL Nat. Microbiol. 6:594-605(2021).
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 (By similarity). Binds GTP and shows GTPase
CC activity, but only at high salt (2 M KCl) concentrations
CC (PubMed:8858586). Involved in division ring assembly directing the
CC assembly, positioning and stabilization of FtsZ2 at the midcell
CC envelope. Plays a role in defining cell shape (PubMed:33903747).
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747,
CC ECO:0000269|PubMed:8858586}.
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 ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513,
CC ECO:0000269|PubMed:8858586}. Note=Assembles at midcell at the inner
CC surface of the cytoplasmic membrane. {ECO:0000269|PubMed:33903747,
CC ECO:0000269|PubMed:34103513, ECO:0000269|PubMed:8858586}.
CC -!- DISRUPTION PHENOTYPE: Viable, but have fewer colony-forming units
CC compared to wild-type. Cells are very heterogeneously sized and
CC misshapen, and have a notable amount of cellular debris. Defects in
CC cell division. Loss or very weak Z2 ring formation. FtsZ1/FtsZ2 double
CC deletion mutant cells show various division defects, including
CC fragmentation, budding, polar tubulation and fission resulting in DNA-
CC containing particles, which are able to remain viable and propagate
CC without regular cell division. {ECO:0000269|PubMed:33903747}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-36 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U37584; AAC44231.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001956; ADE02725.1; -; Genomic_DNA.
DR RefSeq; WP_004044220.1; NZ_AOHU01000097.1.
DR AlphaFoldDB; Q48327; -.
DR SMR; Q48327; -.
DR STRING; 309800.C498_15148; -.
DR EnsemblBacteria; ADE02725; ADE02725; HVO_0717.
DR GeneID; 8925073; -.
DR KEGG; hvo:HVO_0717; -.
DR eggNOG; arCOG02201; Archaea.
DR HOGENOM; CLU_024865_0_1_2; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 41117at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0032153; C:cell division site; IC:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
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 GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
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; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Septation.
FT CHAIN 1..379
FT /note="Cell division protein FtsZ 1"
FT /id="PRO_0000114400"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 146..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT MUTAGEN 250
FT /note="D->A: Defective in cell division inhibiting ring
FT formation. Is not able to complement the deletion mutant of
FT this gene."
FT /evidence="ECO:0000269|PubMed:33903747"
SQ SEQUENCE 379 AA; 39805 MW; BFDEFBDDFE8D0739 CRC64;
MDSIVGDAID EAEAEDMGDE SAQVDGAANI NRSGTMTDDE LKAVLKDLQT NITVVGCGGA
GGNTVNRMHE EGIKGAKLVA ANTDVQHLVE IGADTKILMG EQKTQGRGAG SLPQVGEEAA
LESQEEIYDA IEGSDMVFVT AGLGGGTGTG SAPVVAKAAR ESGALTIAIV TTPFTAEGEV
RRTNAEAGLE RLRDVSDTVI VVPNDRLLDA VGKLPVRQAF KVSDEVLMRS VKGITELITK
PGLVNLDFAD VKTVMERGGV AMIGLGESDS ESKAQESVKS ALRSPLLDVD ISGANSALVN
VTGGSDMSIE EAEGVVEEIY DRIDPDARII WGTSVDDELE GMMRTMIVVT GVESPQIYGR
NGEAQAHAEE RLEDIDYVE
