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ERA_HELPY
ID   ERA_HELPY               Reviewed;         301 AA.
AC   P56059; P96520;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=HP_0517;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Akopyants N.S., Kersulyte D., Clifton S.W., Youree B.E., Reece C.A.,
RA   Roe B.A., Berg D.E.;
RT   "The Cag pathogenicity island of Helicobacter pylori.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD07585.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000511; AAD07585.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AC000108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; E64584; E64584.
DR   RefSeq; NP_207314.1; NC_000915.1.
DR   RefSeq; WP_001862438.1; NC_000915.1.
DR   AlphaFoldDB; P56059; -.
DR   SMR; P56059; -.
DR   STRING; 85962.C694_02660; -.
DR   PaxDb; P56059; -.
DR   EnsemblBacteria; AAD07585; AAD07585; HP_0517.
DR   KEGG; hpy:HP_0517; -.
DR   PATRIC; fig|85962.47.peg.556; -.
DR   eggNOG; COG1159; Bacteria.
DR   OMA; WAEVDVI; -.
DR   PhylomeDB; P56059; -.
DR   Proteomes; UP000000429; 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   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..301
FT                   /note="GTPase Era"
FT                   /id="PRO_0000180018"
FT   DOMAIN          4..173
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          204..280
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
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          64..67
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          122..125
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         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   CONFLICT        55
FT                   /note="W -> G (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="S -> N (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="Q -> K (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="D -> S (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="A -> D (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="A -> T (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169..170
FT                   /note="QH -> KY (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="N -> S (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296..297
FT                   /note="HR -> YQ (in Ref. 2; AC000108)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  34591 MW;  BB9283013A3AA07C CRC64;
     MKTKAGFVAL IGKPNAGKST LLNTLLNAHL ALVSHKANAT RKLMKCIVPF KDKEWYESQI
     IFLDTPGLHH QEKLLNQCML SQALKAMGDA ELCVFLASVH DDLKGYEEFL SLCQKPHILA
     LSKIDTATHK QVLQKLQEYQ QYDSQFLALV PLSAKKSQNL NALLECISQH LSPSAWLFEK
     DLMSDEKMRD IYKEIIRESL FDFLSDEIPY ESDVMIDKFI EEERIDKVYA RIIVEKESQK
     KIVIGKNGVN IKRIGTNARL KMQEVGEKKV FLNLQVIAQK SWSKEEKSLQ KLGYIHRRNR
     D
 
 
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