CETZ2_HALVD
ID CETZ2_HALVD Reviewed; 360 AA.
AC D4GTC1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Tubulin-like protein CetZ2 {ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog 2 {ECO:0000303|PubMed:25533961};
GN Name=cetZ2 {ECO:0000303|PubMed:25533961};
GN Synonyms=ftsZ3 {ECO:0000312|EMBL:ADE04817.1};
GN OrderedLocusNames=HVO_0745 {ECO:0000312|EMBL:ADE04817.1};
GN ORFNames=C498_15008 {ECO:0000312|EMBL:ELY26392.1};
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 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=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-349 AND 350-360 IN COMPLEX WITH
RP GTP ANALOG, FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-212.
RX PubMed=25533961; DOI=10.1038/nature13983;
RA Duggin I.G., Aylett C.H., Walsh J.C., Michie K.A., Wang Q., Turnbull L.,
RA Dawson E.M., Harry E.J., Whitchurch C.B., Amos L.A., Loewe J.;
RT "CetZ tubulin-like proteins control archaeal cell shape.";
RL Nature 519:362-365(2015).
CC -!- FUNCTION: Involved in cell shape control. {ECO:0000255|HAMAP-
CC Rule:MF_01946, ECO:0000269|PubMed:25533961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01946}.
CC -!- DISRUPTION PHENOTYPE: Does not affect motility. No differences in
CC growth rate or cell size. {ECO:0000269|PubMed:25533961}.
CC -!- SIMILARITY: Belongs to the CetZ family. {ECO:0000255|HAMAP-
CC Rule:MF_01946, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001956; ADE04817.1; -; Genomic_DNA.
DR EMBL; AOHU01000097; ELY26392.1; -; Genomic_DNA.
DR RefSeq; WP_004044192.1; NZ_AOHU01000097.1.
DR PDB; 4B45; X-ray; 2.10 A; A=1-349, B=350-360.
DR PDBsum; 4B45; -.
DR AlphaFoldDB; D4GTC1; -.
DR SMR; D4GTC1; -.
DR STRING; 309800.C498_15008; -.
DR EnsemblBacteria; ADE04817; ADE04817; HVO_0745.
DR EnsemblBacteria; ELY26392; ELY26392; C498_15008.
DR GeneID; 8925085; -.
DR KEGG; hvo:HVO_0745; -.
DR PATRIC; fig|309800.29.peg.2896; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR OMA; LYQANAG; -.
DR OrthoDB; 23481at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR HAMAP; MF_01946; CetZ; 1.
DR InterPro; IPR032907; CetZ.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell shape; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..360
FT /note="Tubulin-like protein CetZ2"
FT /id="PRO_0000432184"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 65..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25533961"
FT BINDING 106..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT MUTAGEN 212
FT /note="E->A: Reduces motility. Produces a high-curvature
FT phenotype."
FT /evidence="ECO:0000269|PubMed:25533961"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:4B45"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 175..196
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:4B45"
FT HELIX 323..340
FT /evidence="ECO:0007829|PDB:4B45"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4B45"
SQ SEQUENCE 360 AA; 37109 MW; 2AE9AEDF56AC98E4 CRC64;
MKTVLIGVGQ AGGKLASALQ SFDRQTGFGA VLDAVAVNTA KADLQSLPVE TVLIGQDRVN
GHGVGGDNEL GAAVMESDQT EVMSALDGRV TAEAESIFVV AGLGGGSGSG GAPVLAKALA
GVYDVPVYVL GILPGADEGA LYQVNAGRSL KTVAREADAV LLVDNDAFRS AGESMSEGYD
AINEAIARRV GLLLAAGEAT EGVGESVVDT SEVINTLRSG GIAALGYASA EASPNAEDNI
NAVMSTTRRA VLTGTSLPDA SDADAALVVI AGEPDTIPRK GVERARRWVE DETGSMQVRG
GDFPLESGRL ASLVLLGGVE RSERVESFME RAREAIDKAE TEPREDPKGM WHSDDLDDLL
