CETZ3_HALVD
ID CETZ3_HALVD Reviewed; 389 AA.
AC D4GW48;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Tubulin-like protein CetZ3 {ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog 3 {ECO:0000303|PubMed:25533961};
GN Name=cetZ3 {ECO:0000303|PubMed:25533961};
GN Synonyms=ftsZ5 {ECO:0000312|EMBL:ADE04596.1};
GN OrderedLocusNames=HVO_1113 {ECO:0000312|EMBL:ADE04596.1};
GN ORFNames=C498_13178 {ECO:0000312|EMBL:ELY28197.1};
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 DISRUPTION PHENOTYPE.
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}.
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}.
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DR EMBL; CP001956; ADE04596.1; -; Genomic_DNA.
DR EMBL; AOHU01000091; ELY28197.1; -; Genomic_DNA.
DR RefSeq; WP_004043824.1; NZ_AOHU01000091.1.
DR AlphaFoldDB; D4GW48; -.
DR SMR; D4GW48; -.
DR STRING; 309800.C498_13178; -.
DR EnsemblBacteria; ADE04596; ADE04596; HVO_1113.
DR EnsemblBacteria; ELY28197; ELY28197; C498_13178.
DR GeneID; 8923903; -.
DR KEGG; hvo:HVO_1113; -.
DR PATRIC; fig|309800.29.peg.2530; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR OMA; IHEIDAF; -.
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: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 3: Inferred from homology;
KW Cell shape; Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..389
FT /note="Tubulin-like protein CetZ3"
FT /id="PRO_0000432185"
FT BINDING 10..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT BINDING 110..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT BINDING 169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
SQ SEQUENCE 389 AA; 40858 MW; C01D9CE56913B41F CRC64;
MKLALIGIGQ AGGKVVDALV DYERRTKTGF VVDAIAVNSA RADLRGLRTA PESRQVLVGL
TRVKGHGVGA DNELGAEVIA EDVGEVLSMI DDLPVHEIDA FLVVAGLGGG TGSGGAPVIA
RELKHIYTEP VYGLGILPAR DEGGIYTLNA ARSFQTFVRE VDNLIVFDND AWRKTGESLE
AGYGSLNAEL ARRLGVLFSA GEGDGSGAVA ESVVDASEII NTLGSGGVST IGYAAVELDR
PKRGLLSRLS GGKAEADDGG DSTNRITSLV RRAALGRLTL PCEISGAERG LVVVAGPSDV
LSRRGIERAR TWLEDETGTM EIRGGDYPID SNFVAAVVLL SGVYDVPRVK ELQAVAIETQ
RDMLAKRESS AASLDDLVST GDDRIEPLF