ERA_STRR6
ID ERA_STRR6 Reviewed; 299 AA.
AC P0A3C4; Q9XDG9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=GTPase Era;
GN Name=era; OrderedLocusNames=spr0871;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS GTPASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND ABILITY TO COMPLEMENT E.COLI
RP DISRUPTION MUTANT.
RX PubMed=10220158; DOI=10.1099/13500872-145-4-791;
RA Zhao G., Meier T.I., Peery R.B., Matsushima P., Skatrud P.L.;
RT "Biochemical and molecular analyses of the C-terminal domain of Era GTPase
RT from Streptococcus pneumoniae.";
RL Microbiology 145:791-800(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP FUNCTION AS GTPASE, SMALL RRNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=14519129; DOI=10.1046/j.1432-1033.2003.03813.x;
RA Hang J.Q., Zhao G.;
RT "Characterization of the 16S rRNA- and membrane-binding domains of
RT Streptococcus pneumoniae Era GTPase: structural and functional
RT implications.";
RL Eur. J. Biochem. 270:4164-4172(2003).
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). Complements an E.coli era
CC disruption mutant. Binds 16S rRNA as well as poly(U) RNA, binding to
CC the latter is inhibited by liposomes. {ECO:0000250,
CC ECO:0000269|PubMed:10220158, ECO:0000269|PubMed:14519129}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=430 uM for GTP {ECO:0000269|PubMed:10220158};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein.
CC -!- DOMAIN: The Era-type G (guanine nucleotide-binding) domain has GTPase
CC activity, while the C-terminal KH type-2 domain is required for 16S
CC rRNA binding and for membrane localization. Neither rRNA binding nor
CC membrane localization require the N-terminal G domain, and the GTPase
CC does not require the KH domain.
CC -!- MISCELLANEOUS: It is estimated there is 0.63 ng Era per ug total cell
CC protein in this strain.
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}.
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DR EMBL; AF072811; AAD41632.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99675.1; -; Genomic_DNA.
DR PIR; G97980; G97980.
DR RefSeq; NP_358465.1; NC_003098.1.
DR RefSeq; WP_000143265.1; NC_003098.1.
DR AlphaFoldDB; P0A3C4; -.
DR SMR; P0A3C4; -.
DR STRING; 171101.spr0871; -.
DR EnsemblBacteria; AAK99675; AAK99675; spr0871.
DR GeneID; 60233990; -.
DR KEGG; spr:spr0871; -.
DR PATRIC; fig|171101.6.peg.959; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_9; -.
DR OMA; WAEVDVI; -.
DR SABIO-RK; P0A3C4; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
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_0000180059"
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 REGION 232..299
FT /note="Required to associate with cell membrane, for
FT complmentation of E.coli disruption, increases affinity for
FT GTP but decreases GTP hydrolysis"
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"
SQ SEQUENCE 299 AA; 34010 MW; E00E79B274C00A4C CRC64;
MTFKSGFVAI LGRPNVGKST FLNHVMGQKI AIMSDKAQTT RNKIMGIYTT DKEQIVFIDT
PGIHKPKTAL GDFMVESAYS TLREVDTVLF MVPADEARGK GDDMIIERLK AAKVPVILVV
NKIDKVHPDQ LLSQIDDFRN QMDFKEIVPI SALQGNNVSR LVDILSENLD EGFQYFPSDQ
ITDHPERFLV SEMVREKVLH LTREEIPHSV AVVVDSMKRD EETDKVHIRA TIMVERDSQK
GIIIGKGGAM LKKIGSMARR DIELMLGDKV FLETWVKVKK NWRDKKLDLA DFGYNEREY
