FTSZ2_HALVD
ID FTSZ2_HALVD Reviewed; 400 AA.
AC D4GSH7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=HVO_0581;
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 [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 [2]
RP SUBUNIT, AND 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP ASP-231, 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. Binds GTP and shows GTPase activity (By
CC similarity). Required for division ring constriction (PubMed:33903747).
CC {ECO:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:33903747}.
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 (By similarity). Interacts with SepF
CC (PubMed:34103513). {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:34103513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909,
CC ECO:0000269|PubMed:33903747, ECO:0000269|PubMed:34103513}.
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. Loss of cell
CC division. No effect on Z1 ring formation. FtsZ1/FtsZ2 double deletion
CC mutant cells show various division defects, including fragmentation,
CC budding, polar tubulation and fission resulting in DNA-containing
CC particles, which are able to remain viable and propagate without
CC regular cell division. {ECO:0000269|PubMed:33903747}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00909}.
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DR EMBL; CP001956; ADE02657.1; -; Genomic_DNA.
DR RefSeq; WP_004044352.1; NZ_AOHU01000098.1.
DR AlphaFoldDB; D4GSH7; -.
DR SMR; D4GSH7; -.
DR STRING; 309800.C498_15820; -.
DR EnsemblBacteria; ADE02657; ADE02657; HVO_0581.
DR GeneID; 8926446; -.
DR KEGG; hvo:HVO_0581; -.
DR eggNOG; arCOG02201; Archaea.
DR HOGENOM; CLU_024865_0_1_2; -.
DR OMA; IMNQGGV; -.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0036213; P:contractile ring contraction; 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 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 Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Septation.
FT CHAIN 1..400
FT /note="Cell division protein FtsZ 2"
FT /id="PRO_0000414242"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 128..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT MUTAGEN 231
FT /note="D->A: Defective in cell division inhibiting ring
FT constriction. Is not able to complement the deletion mutant
FT of this gene."
FT /evidence="ECO:0000269|PubMed:33903747"
SQ SEQUENCE 400 AA; 42570 MW; 2CCBBFF5AA4CA4DE CRC64;
MQDIVREAME RDEAERQTQS SLEDSDDQFG DPRIVIVGAG GAGNNTINRL YNIGVEGADT
VAINTDKQHL KMIEADTKIL VGKSLTQGLG AGGDPSMGER ATEMAQGTIK DVLGDADLVF
VTAGMGGGTG TGAAPVVAKI AKEQGAIVVG MVSTPFNVER ARTVKAEEGL ENLRNEADSI
IVLDNNRLLD YVPNLPIGKA FSVMDQIIAE TVKGISETIT QPSLINLDYA DMSTIMNQGG
VAVMLVGETQ DKNKTQEVVN DAMNHPLLDV DYRGASGGLV HITGGPDLTL KEAEGIASNI
TERLEAAANV IWGARIQDEY KGKVRVMAIM TGVQSAQVLG PSTQKQADKS RQSIQSRESQ
QQHSGSEFDS SERAQTAQSG TWSDGGRDEV EKNNGLDVIR
