CETZ4_HALVD
ID CETZ4_HALVD Reviewed; 394 AA.
AC D4GQ67;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Tubulin-like protein CetZ4 {ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog 4 {ECO:0000303|PubMed:25533961};
GN Name=cetZ4 {ECO:0000303|PubMed:25533961};
GN Synonyms=ftsZ6 {ECO:0000312|EMBL:ADE01805.1};
GN OrderedLocusNames=HVO_A0035 {ECO:0000312|EMBL:ADE01805.1};
GN ORFNames=C498_11071 {ECO:0000312|EMBL:ELY28675.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4 {ECO:0000312|EMBL:ADE01805.1}.
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; CP001955; ADE01805.1; -; Genomic_DNA.
DR EMBL; AOHU01000087; ELY28675.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GQ67; -.
DR SMR; D4GQ67; -.
DR STRING; 309800.C498_11071; -.
DR EnsemblBacteria; ADE01805; ADE01805; HVO_A0035.
DR EnsemblBacteria; ELY28675; ELY28675; C498_11071.
DR KEGG; hvo:HVO_A0035; -.
DR PATRIC; fig|309800.29.peg.2114; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR Proteomes; UP000008243; Plasmid pHV4.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..394
FT /note="Tubulin-like protein CetZ4"
FT /id="PRO_0000432186"
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; 41158 MW; 6B95BC1AD6D02245 CRC64;
MKLGVVGLGQ AGGKIVDALL EYDQRTNCHI VHDALTVNTA TADLNALEHI PADARVLIGK
SQVGGQGVGG DNELGATITT EDITEIQHVI DTISVHEIDA FLLVAALGGG TGSGALPVVG
RHLKQLYTEP VYGLGILPST NEGGLYSLNA ARSLQTAVRE LDNLLIFDND AHRQANESLT
GGYAAINREL ATRLGVLFGA GDIDTGTANP ESVVDASEII NTLKGGGVST LGYASQSLEE
EDGAEAAGLL SRFKRESSTD SAGGTNRITS LVRRATLGRL TLPVEPANVS IDRGLVIVAG
PSDCLNRKGI ERGRTWVEEQ TGCLSIRGGD YPLPESNTVA VVVLFSGISG ADRLHELRSI
GSEAQTTGAE RTGSSDRHLE SILGDDADEL DSLF
