ID Q3IRF0_NATPD Unreviewed; 392 AA.
AC Q3IRF0;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN Name=cetZ1 {ECO:0000313|EMBL:CAI49293.1};
GN Synonyms=cetZ {ECO:0000256|HAMAP-Rule:MF_01946}, ftsZ4
GN {ECO:0000313|EMBL:CAI49293.1};
GN OrderedLocusNames=NP_2404A {ECO:0000313|EMBL:CAI49293.1};
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:CAI49293.1, ECO:0000313|Proteomes:UP000002698};
RN [1] {ECO:0000313|EMBL:CAI49293.1, 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; CAI49293.1; -; Genomic_DNA.
DR RefSeq; WP_011322919.1; NC_007426.1.
DR AlphaFoldDB; Q3IRF0; -.
DR STRING; 348780.NP_2404A; -.
DR EnsemblBacteria; CAI49293; CAI49293; NP_2404A.
DR GeneID; 3702730; -.
DR KEGG; nph:NP_2404A; -.
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 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 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Basic and 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 392 AA; 41919 MW; 24292E84B094F526 CRC64;
MKLAMIGFGQ AGGKILDRFL EYDSTRGTGI VGHAVAVNSA KADLMGLDYV PNENRVLIGQ
SVVKGHGAGT EPELGERCAK EDMEEIQSAI DRMVSSEIDA FLVMAGLGGG TGSGGAPVLA
EHLQRLYVEP VYGLGILPAR DEGGIYNRNA ARSFQRFAEA VDNLLTFDND AFKTGGESLG
EGYAEINAEI ITRFGALFSA GEVEALGDNV AESVVDASEI INTLGEHGIS SVGYASEPVQ
TKQQSSGLLD RLRGGNDKNG FSSGGDATNR ITSLVRKATL GKLTLQCEVD STERVLLLVS
GPPEALNRKG IDKARKWLES QTDCMEVRAG DYPLPNEDKV AAIVVLSGVT DVPRVKEMQR
MAVEAEEKVE EIRSQSKDDL DDLIEYGDDE TQ
//
