ID Q3IRT7_NATPD Unreviewed; 396 AA.
AC Q3IRT7;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN Name=cetZ2 {ECO:0000313|EMBL:CAI49155.1};
GN Synonyms=cetZ {ECO:0000256|HAMAP-Rule:MF_01946}, ftsZ3
GN {ECO:0000313|EMBL:CAI49155.1};
GN OrderedLocusNames=NP_2128A {ECO:0000313|EMBL:CAI49155.1};
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780 {ECO:0000313|EMBL:CAI49155.1, ECO:0000313|Proteomes:UP000002698};
RN [1] {ECO:0000313|EMBL:CAI49155.1, ECO:0000313|Proteomes:UP000002698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC NCIMB 2260 / Gabara {ECO:0000313|Proteomes:UP000002698};
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- FUNCTION: Involved in cell shape control. {ECO:0000256|HAMAP-
CC Rule:MF_01946}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01946}.
CC -!- SIMILARITY: Belongs to the CetZ family. {ECO:0000256|ARBA:ARBA00006877,
CC ECO:0000256|HAMAP-Rule:MF_01946}.
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DR EMBL; CR936257; CAI49155.1; -; Genomic_DNA.
DR RefSeq; WP_011322783.1; NC_007426.1.
DR AlphaFoldDB; Q3IRT7; -.
DR STRING; 348780.NP_2128A; -.
DR EnsemblBacteria; CAI49155; CAI49155; NP_2128A.
DR GeneID; 3702729; -.
DR KEGG; nph:NP_2128A; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR OrthoDB; 329751at2157; -.
DR Proteomes; UP000002698; Chromosome.
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 CDD; cd02202; CetZ_tubulin-like; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR HAMAP; MF_01946; CetZ; 1.
DR InterPro; IPR032907; CetZ.
DR InterPro; IPR048737; CetZ_C.
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; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR PANTHER; PTHR30314:SF10; TUBULIN-LIKE PROTEIN CETZ; 1.
DR Pfam; PF21011; CetZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_01946}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01946};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01946};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01946}; Reference proteome {ECO:0000313|Proteomes:UP000002698}.
FT DOMAIN 2..195
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT REGION 357..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 110..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ SEQUENCE 396 AA; 40751 MW; B2B9D9D9D36D2009 CRC64;
MKLVAIGAGQ AGGKVLDRLL EHDARHPGTF LAHAVAVNTA EPDLQALDAV PEESRLLIGQ
STVGGHGTGT DPETGRECAR EAESEIQSAI DHAPTSSIDG FVVIAGLGGG TGSGAAPVIA
ERLRAVYAEP VYGLGILPTA DEGGLYSRNA ADSLQAFVGA TDGLLVFDND AFKSSGETLS
EGYGAINEEI ATRFGTLFSA GELEALGDDI AESVVDASEI INTLEGLVSV GYASEELPDD
AGDDGGLLGR VLGGSDDDSI GSDAVVQIPA LVRRAALGKL TLPCNLASTS KALLIVAGPP
EHLSRKGIDN ARSWLESEID CREVRAGDYP LPDADRVAAL VVLSGVTDVP RIDRMQSQAV
DAETAETSEA ESEDAMQDLI EYGDDSDGDG ATDGHT
//
