CETZ5_HALVD
ID CETZ5_HALVD Reviewed; 394 AA.
AC D4GU26; L9VC10;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Tubulin-like protein CetZ5 {ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog 5 {ECO:0000303|PubMed:25533961};
GN Name=cetZ5 {ECO:0000303|PubMed:25533961};
GN Synonyms=ftsZ7 {ECO:0000312|EMBL:ADE03513.1};
GN OrderedLocusNames=HVO_2013 {ECO:0000312|EMBL:ADE03513.1};
GN ORFNames=C498_05346 {ECO:0000312|EMBL:ELY34527.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ELY34527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001956; ADE03513.1; -; Genomic_DNA.
DR EMBL; AOHU01000038; ELY34527.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; D4GU26; -.
DR SMR; D4GU26; -.
DR STRING; 309800.C498_05346; -.
DR EnsemblBacteria; ADE03513; ADE03513; HVO_2013.
DR EnsemblBacteria; ELY34527; ELY34527; C498_05346.
DR KEGG; hvo:HVO_2013; -.
DR PATRIC; fig|309800.29.peg.1043; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR OMA; QWLEDET; -.
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..394
FT /note="Tubulin-like protein CetZ5"
FT /id="PRO_0000432187"
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 394 AA; 41500 MW; 434F77E3AE549CC5 CRC64;
MKVLCFGMGQ AGGNVLDALL RYEQRTNADY VVDAVAYNTA SADLRGLDLV PEENRILFGA
DEVSGHGVGA DNELAAELAE RDSRQLLRGT DGAPTSTADA FLIFAGLGGG TGSGAAPVLA
KHLNRIYEQP IYGVGILPAA DEGALYSRNA ARSLKALVDV TDHVFAFDNG AWAESGEDVA
QAHDTMNEVL VRRLGILFAS GEVAESGTVA ESVVDSSEVI NTLRGGGIST IGYAASELPE
SDGGGGFSIK GLLGGDSSST DELDSINRIT TQTRKAVLGQ LTLPCDVDSA SRGLVVVSGP
PEWLNRKAVE RSRTWVEEQT GSMEVRGGDY PLSESNHVGV LVLLGDVSRS DRVAEIRSTA
VEAEQNRRER IASDAADRED GTEAVVDDRL DSLF
