DER_STRMU
ID DER_STRMU Reviewed; 436 AA.
AC Q8DS90; Q9RHV5;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA, serA;
GN OrderedLocusNames=SMU_1920;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MT8148 / Serotype c;
RX PubMed=11155166; DOI=10.1034/j.1399-302x.2000.150110.x;
RA Kawabata S., Terao Y., Hamada S.;
RT "Molecular cloning, sequence and characterization of a novel streptococcal
RT phosphoglycerate dehydrogenase gene.";
RL Oral Microbiol. Immunol. 15:58-62(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
CC -!- CAUTION: Was originally thought to be a D-3-phosphoglycerate
CC dehydrogenase. {ECO:0000305|PubMed:11155166}.
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DR EMBL; AB016077; BAA88823.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59531.1; -; Genomic_DNA.
DR RefSeq; NP_722225.1; NC_004350.2.
DR RefSeq; WP_002262117.1; NC_004350.2.
DR AlphaFoldDB; Q8DS90; -.
DR SMR; Q8DS90; -.
DR STRING; 210007.SMU_1920; -.
DR PRIDE; Q8DS90; -.
DR EnsemblBacteria; AAN59531; AAN59531; SMU_1920.
DR KEGG; smu:SMU_1920; -.
DR PATRIC; fig|210007.7.peg.1706; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_9; -.
DR OMA; KFRFLEY; -.
DR PhylomeDB; Q8DS90; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTP-bd_EngA.
DR InterPro; IPR032859; KH_dom-like.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 2.
DR PROSITE; PS51712; G_ENGA; 2.
PE 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..436
FT /note="GTPase Der"
FT /id="PRO_0000179054"
FT DOMAIN 4..167
FT /note="EngA-type G 1"
FT DOMAIN 175..351
FT /note="EngA-type G 2"
FT DOMAIN 352..436
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 181..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 229..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 294..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT CONFLICT 165
FT /note="T -> A (in Ref. 1; BAA88823)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="A -> T (in Ref. 1; BAA88823)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> S (in Ref. 1; BAA88823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48586 MW; 24D8428A91C2A097 CRC64;
MALPTVAIVG RPNVGKSALF NRIAGERISI VEDVEGVTRD RIYTKAEWLN RQFSIIDTGG
IDDVDAPFME QIKHQADIAM TEADVIVFVV SAKEGITDAD EYVAKILYRT HKPVILAVNK
VDNPEMRSAI YDFYALGLGD PYPVSSAHGI GTGDVLDAIV DNLPTEAQEE SSDIIKFSLI
GRPNVGKSSL INAILGEDRV IASPVAGTTR DAIDTTFTDE EGQEFTMIDT AGMRKSGKVY
ENTEKYSVMR AMRAIDRSDI VLMVLNAEEG IREYDKRIAG FAHEAGKGIV VVVNKWDAIK
KDNRTVAQWE ADIRDNFQYI PYAPIVFVSA VTKQRLHKLP DVIKQVSQSQ NTRIPSAVLN
DVVMDAVAIN PTPTDKGKRL KIFYATQVSV KPPTFVIFVN EEELMHFSYL RFLENQIRQA
FVFEGTPIRL IARKRK
