CETZ1_HALVD
ID CETZ1_HALVD Reviewed; 395 AA.
AC D4GVD7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Tubulin-like protein CetZ1 {ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog 1 {ECO:0000303|PubMed:25533961};
GN Name=cetZ1 {ECO:0000303|PubMed:25533961};
GN Synonyms=ftsZ4 {ECO:0000312|EMBL:ADE04578.1};
GN OrderedLocusNames=HVO_2204 {ECO:0000312|EMBL:ADE04578.1};
GN ORFNames=C498_06313 {ECO:0000312|EMBL:ELY33433.1};
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 (1.90 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-218.
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. Essential for the development
CC of a rod-shaped cell type required for efficient swimming.
CC {ECO:0000269|PubMed:25533961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01946,
CC ECO:0000269|PubMed:25533961}. Note=In plates, seen throughout the
CC cytoplasm. Localized as spots, short filaments at or near the envelope.
CC In motile rods, localized at or near one or both poles, as spots, short
CC filaments or end-caps, and at mid-cell. {ECO:0000269|PubMed:25533961}.
CC -!- DISRUPTION PHENOTYPE: Swimming defect. No differences in growth rate or
CC 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; ADE04578.1; -; Genomic_DNA.
DR EMBL; AOHU01000041; ELY33433.1; -; Genomic_DNA.
DR PDB; 4B46; X-ray; 1.90 A; A=1-395.
DR PDBsum; 4B46; -.
DR AlphaFoldDB; D4GVD7; -.
DR SMR; D4GVD7; -.
DR STRING; 309800.C498_06313; -.
DR EnsemblBacteria; ADE04578; ADE04578; HVO_2204.
DR EnsemblBacteria; ELY33433; ELY33433; C498_06313.
DR KEGG; hvo:HVO_2204; -.
DR PATRIC; fig|309800.29.peg.1233; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR OMA; TNVPRIK; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; 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; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF00091; Tubulin; 1.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell shape; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..395
FT /note="Tubulin-like protein CetZ1"
FT /id="PRO_0000432183"
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 110..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT MUTAGEN 218
FT /note="E->A: Reduces motility. Does not form rods. No
FT division defect."
FT /evidence="ECO:0000269|PubMed:25533961"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 9..26
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 179..198
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 265..280
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:4B46"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:4B46"
FT HELIX 353..366
FT /evidence="ECO:0007829|PDB:4B46"
SQ SEQUENCE 395 AA; 42064 MW; 871388F2F58AA8D9 CRC64;
MKLAMIGFGQ AGGKVVDKFV EYDRERNAGI VRAAVAVNSA KADLLGLKNI PKDQRVLIGQ
SRVKGHGVGA DNELGAEIAE EDIDEVQGAI DSIPVHEVDA FLVVSGLGGG TGSGGAPVLA
KHLKRIYTEP VYGLGILPGS DEGGIYTLNA ARSFQTFVRE VDNLLVFDND AWRKTGESVQ
GGYDEINEEI VNRFGVLFGA GEVQDGQEVA ESVVDSSEII NTLAGGGVST VGYASEGVEP
RKNNGGGLLS RLTGGDEPDD NLDTAHTTNR ITSLVRKAAL GRLTLPCEIE GAERALLVLA
GPPEHLNRKG IERGRKWIEE QTGSMEVRGG DYPIPGAEKV AGVILLSGVT NVPRIKELQQ
VAIEAQDNIE EIRQESDSNL ETLINDDEDE LESLF
