ERA_THET8
ID ERA_THET8 Reviewed; 301 AA.
AC Q5SM23;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=GTPase Era;
GN Name=era; OrderedLocusNames=TTHA0120;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (13.50 ANGSTROMS), INTERACTION WITH 30S
RP RIBOSOMAL SUBUNIT, RIBOSOMAL PROTEINS S2; S7; S11 AND S18, AND SMALL
RP RRNA-BINDING.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15866174; DOI=10.1016/j.molcel.2005.03.028;
RA Sharma M.R., Barat C., Wilson D.N., Booth T.M., Kawazoe M.,
RA Hori-Takemoto C., Shirouzu M., Yokoyama S., Fucini P., Agrawal R.K.;
RT "Interaction of Era with the 30S ribosomal subunit implications for 30S
RT subunit assembly.";
RL Mol. Cell 18:319-329(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH A GUANINE
RP NUCLEOTIDE.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Kawazoe M., Hori-Takemoto C., Kaminishi T., Sekine S., Shirouzu M.,
RA Yokoyama S.;
RT "Crystal structure of GTP-binding protein TT1341 from Thermus thermophilus
RT HB8.";
RL Submitted (FEB-2009) to the PDB data bank.
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). {ECO:0000250}.
CC -!- FUNCTION: The Era binding site on the 30S subunit overlaps that of
CC protein S1 and is in direct contact with 5 nucleotides directly
CC upstream of the anti-Shine-Dalgarno sequence; the presence of Era may
CC prevent mRNA recruitment. 30S subunits bound to Era are not able to
CC bind to the 50S subunit to make functional ribosomes. Era may serve a
CC role in the final stages of 30S ribosomal subunit assembly.
CC -!- SUBUNIT: Monomer (Probable). Binds to the 30S ribosomal subunit,
CC between the head and platform, contacting the 16S rRNA. Contacts
CC ribosomal proteins S7 and S18 and may contact proteins S2 and S11.
CC {ECO:0000269|Ref.3, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
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; AP008226; BAD69943.1; -; Genomic_DNA.
DR RefSeq; WP_008630929.1; NC_006461.1.
DR RefSeq; YP_143386.1; NC_006461.1.
DR PDB; 1WF3; X-ray; 1.88 A; A=1-301.
DR PDB; 1X18; EM; 13.50 A; X=1-301.
DR PDB; 1X1L; EM; 13.50 A; X=1-301.
DR PDBsum; 1WF3; -.
DR PDBsum; 1X18; -.
DR PDBsum; 1X1L; -.
DR AlphaFoldDB; Q5SM23; -.
DR SMR; Q5SM23; -.
DR STRING; 300852.55771502; -.
DR EnsemblBacteria; BAD69943; BAD69943; BAD69943.
DR GeneID; 3167951; -.
DR KEGG; ttj:TTHA0120; -.
DR PATRIC; fig|300852.9.peg.118; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_0; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; Q5SM23; -.
DR EvolutionaryTrace; Q5SM23; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:UniProtKB.
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 PRINTS; PR00326; GTP1OBG.
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 3D-structure; Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding;
KW Membrane; Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..301
FT /note="GTPase Era"
FT /id="PRO_0000403972"
FT DOMAIN 6..173
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 205..282
FT /note="KH type-2"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 40..44
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 61..64
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 125..128
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 152..154
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1WF3"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:1WF3"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 251..268
FT /evidence="ECO:0007829|PDB:1WF3"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1WF3"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:1WF3"
SQ SEQUENCE 301 AA; 33809 MW; E5403580A8D161F5 CRC64;
MAEKTYSGFV AIVGKPNVGK STLLNNLLGV KVAPISPRPQ TTRKRLRGIL TEGRRQIVFV
DTPGLHKPMD ALGEFMDQEV YEALADVNAV VWVVDLRHPP TPEDELVARA LKPLVGKVPI
LLVGNKLDAA KYPEEAMKAY HELLPEAEPR MLSALDERQV AELKADLLAL MPEGPFFYPE
DYAKSDQTFG EWVAEILREE AMKRLWHEVP YAVATKVEEV AERENGVLYI KAILYVERPS
QKAIVIGEGG RKIKEIGQAT RKQLEALLGK KVYLDLEVKV YPDWRKDPEA LRELGYRSSV
G
