ERA_STRMU
ID ERA_STRMU Reviewed; 299 AA.
AC P37214;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=GTPase Era;
DE AltName: Full=SGP;
GN Name=era; Synonyms=spg; OrderedLocusNames=SMU_1617;
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=GS-5;
RX PubMed=8407794; DOI=10.1128/jb.175.19.6220-6228.1993;
RA Yamashita Y., Takehara T., Kuramitsu H.K.;
RT "Molecular characterization of a Streptococcus mutans mutant altered in
RT environmental stress responses.";
RL J. Bacteriol. 175:6220-6228(1993).
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).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP GTPASE ACTIVITY, AND NUCLEOTIDE-BINDING.
RC STRAIN=GS-5;
RX PubMed=7790064; DOI=10.1128/iai.63.7.2516-2521.1995;
RA Wu J., Cho M.I., Kuramitsu H.K.;
RT "Expression, purification, and characterization of a novel G protein, SGP,
RT from Streptococcus mutans.";
RL Infect. Immun. 63:2516-2521(1995).
CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid
CC nucleotide exchange. Plays a role in 16S rRNA processing and 30S
CC ribosomal subunit biogenesis and possibly also in cell cycle regulation
CC and energy metabolism (By similarity). Has GTPase activity, binds both
CC GDP and GTP, does not bind UTP, CTP or ATP. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: GTPase activity is inhibited by GDP but not by
CC UTP, CTP, ATP, GMP or cGMP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 uM for GTP {ECO:0000269|PubMed:7790064};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7790064}. Cell
CC membrane {ECO:0000269|PubMed:7790064}; Peripheral membrane protein
CC {ECO:0000269|PubMed:7790064}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L03428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014133; AAN59258.1; -; Genomic_DNA.
DR RefSeq; NP_721952.1; NC_004350.2.
DR RefSeq; WP_002262773.1; NC_004350.2.
DR AlphaFoldDB; P37214; -.
DR SMR; P37214; -.
DR STRING; 210007.SMU_1617; -.
DR EnsemblBacteria; AAN59258; AAN59258; SMU_1617.
DR GeneID; 66819001; -.
DR KEGG; smu:SMU_1617; -.
DR PATRIC; fig|210007.7.peg.1440; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_9; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; P37214; -.
DR SABIO-RK; P37214; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00436; era; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..299
FT /note="GTPase Era"
FT /id="PRO_0000180057"
FT DOMAIN 4..171
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 202..280
FT /note="KH type-2"
FT REGION 12..19
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 38..42
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 59..62
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 121..124
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 150..152
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 129
FT /note="N -> D (in Ref. 1; L03428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34190 MW; 237F88F289C4A00D CRC64;
MSFKSGFVAI LGRPNVGKST FLNHVMGQKI AIMSDKAQTT RNKIMGIYTT DKEQIVFIDT
PGIHKPKTAL GDFMVESAYS TLREVDTVLF MVPADEKRGK GDNMIIERLK AAKVPVILVI
NKIDKVHPNQ LLEQIDDFRN QMDFQEIVPI SALQGNNVSH LVDLLVDHLE EGFQYFPADQ
ITDHPERFLV SEMIREKVLL LTREEIPHSV AVVIDSMARD EETHKIHIRA TIMVERDSQK
GIIIGKKGAM LKKIGQMARR DIELMLGDKV YLETWVKVKK NWRDKKLDLA DFGYNKKEY
