ID ERA_VIBPA Reviewed; 320 AA.
AC Q87LP0;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=VP2571;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00367, ECO:0000255|PROSITE-ProRule:PRU01050}.
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DR EMBL; BA000031; BAC60834.1; -; Genomic_DNA.
DR RefSeq; NP_798950.1; NC_004603.1.
DR RefSeq; WP_005460684.1; NC_004603.1.
DR AlphaFoldDB; Q87LP0; -.
DR SMR; Q87LP0; -.
DR GeneID; 1190095; -.
DR KEGG; vpa:VP2571; -.
DR PATRIC; fig|223926.6.peg.2469; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_2_6; -.
DR Proteomes; UP000002493; Chromosome 1.
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: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 CDD; cd22534; KH-II_Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTPase_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 NCBIfam; TIGR00436; era; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42698; GTPASE ERA; 1.
DR PANTHER; PTHR42698:SF2; GTPASE ERA-LIKE, CHLOROPLASTIC; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..320
FT /note="GTPase Era"
FT /id="PRO_0000180071"
FT DOMAIN 25..193
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 216..302
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 33..40
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 59..63
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 80..83
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 142..145
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 172..174
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 80..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 320 AA; 36566 MW; 0989952E8132ECFF CRC64;
MADNEFDIDA FFASHGEVSS PENQHCGFIA IVGRPNVGKS TLLNKILGQK ISITSRKPQT
TRHRIMGVDT DGDYQAIYVD TPGLHIEEKR AINRLMNRAA NSSLSDVNLV FFLVDGTHWT
KDDEMVLTKL QKSNFPVVLC VNKVDNVQDR NEVMLHMAEM SKKMDFVDVV PISAKQGKNI
DVLRKHVRNH LPKATHHFPE EYVTDRSQRF MASEIVREKL MRFTGDELPY SVTVEIERFD
YNPETDGFHI NALILVERNG QKKMVIGKGG EKIKTIGREA RLDMEELFGR KVYLETWVKV
KSGWADDERA LRSLGYIDDL
//
