CETZ_METTP
ID CETZ_METTP Reviewed; 367 AA.
AC A0B5R2;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000255|HAMAP-Rule:MF_01946, ECO:0000305};
DE AltName: Full=Cell-structure-related euryarchaeota tubulin/FtsZ homolog {ECO:0000303|PubMed:25533961};
GN Name=cetZ {ECO:0000255|HAMAP-Rule:MF_01946, ECO:0000303|PubMed:25533961};
GN OrderedLocusNames=Mthe_0239 {ECO:0000312|EMBL:ABK14036.1};
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP.
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 -!- SIMILARITY: Belongs to the CetZ family. {ECO:0000255|HAMAP-
CC Rule:MF_01946, ECO:0000305}.
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DR EMBL; CP000477; ABK14036.1; -; Genomic_DNA.
DR PDB; 3ZID; X-ray; 2.00 A; A/B=1-367.
DR PDBsum; 3ZID; -.
DR AlphaFoldDB; A0B5R2; -.
DR SMR; A0B5R2; -.
DR STRING; 349307.Mthe_0239; -.
DR EnsemblBacteria; ABK14036; ABK14036; Mthe_0239.
DR KEGG; mtp:Mthe_0239; -.
DR HOGENOM; CLU_745168_0_0_2; -.
DR OMA; QWLEDET; -.
DR Proteomes; UP000000674; Chromosome.
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; 3.40.50.1440; -; 1.
DR HAMAP; MF_01946; CetZ; 1.
DR InterPro; IPR032907; CetZ.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Cell shape; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Tubulin-like protein CetZ"
FT /id="PRO_0000432189"
FT BINDING 11..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25533961"
FT BINDING 115..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT BINDING 194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01946,
FT ECO:0000269|PubMed:25533961"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 10..30
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 79..98
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 186..210
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:3ZID"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3ZID"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:3ZID"
FT HELIX 326..367
FT /evidence="ECO:0007829|PDB:3ZID"
SQ SEQUENCE 367 AA; 41259 MW; D61ADF4070C0F3B5 CRC64;
MLNVLMLGVG QCGNRILDAV NRQAFGGSRL AKYYSKQRFP SRVETIAINT AINDLKELKF
TAAKDRLHVP NLHGVGANRS KGKQGFWENQ EMILEEIEKR GDFDLIFVMT SVSGGTGSSF
SPLMIHELKK RYKNATIVPI AVLPFREEGT IYLQNAAFCL REMIEVEADG MILVDNQYLK
RFSGDIASAY DRINTMVAQR LLFLIEALDS EMLSVTDLGD FKTVMNGGLR MGTLGYYQAD
KKSPSIRAAI KNSLREVGLL YPANVDAGEA GRAMIVIQGS REYLNVDEIT KEIESLTETI
GHVFKGIVIK KGEPRVLSVL SLERAPGLVE LYEKAKWAIQ EERERKDRAR SELYEAFEQI
NDLEEIY
