ID   ERA_COXBU               Reviewed;         295 AA.
AC   P51836;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   15-MAR-2017, entry version 110.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   OrderedLocusNames=CBU_1502;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CB9MIC7;
RX   PubMed=7830573; DOI=10.1111/j.1365-2958.1994.tb01290.x;
RA   Zuber M., Hoover T.A., Powell B.S., Court D.L.;
RT   "Analysis of the rnc locus of Coxiella burnetii.";
RL   Mol. Microbiol. 14:291-300(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Nine Mile Crazy / RSA 514;
RX   PubMed=17088354; DOI=10.1128/IAI.00883-06;
RA   Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D.,
RA   Mead D.J., Samuel J.E., Heinzen R.A.;
RT   "Proteome and antigen profiling of Coxiella burnetii developmental
RT   forms.";
RL   Infect. Immun. 75:290-298(2007).
CC   -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with
CC       rapid nucleotide exchange. Plays a role in 16S rRNA processing and
CC       30S ribosomal subunit biogenesis and possibly also in cell cycle
CC       regulation and energy metabolism. {ECO:0000255|HAMAP-
CC       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   -!- DEVELOPMENTAL STAGE: More than twofold more abundant in the small
CC       cell variant (SCV) stage than in the large cell variant (LCV)
CC       stage (at protein level). LCVs are more metabolically active than
CC       SCVs. {ECO:0000269|PubMed:17088354}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
CC       like GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00367}.
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DR   EMBL; L27436; AAA69691.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO90999.1; -; Genomic_DNA.
DR   PIR; S60768; S60768.
DR   RefSeq; NP_820485.1; NC_002971.3.
DR   RefSeq; WP_010958267.1; NC_002971.3.
DR   ProteinModelPortal; P51836; -.
DR   SMR; P51836; -.
DR   STRING; 227377.CBU_1502; -.
DR   PRIDE; P51836; -.
DR   EnsemblBacteria; AAO90999; AAO90999; CBU_1502.
DR   GeneID; 1209412; -.
DR   KEGG; cbu:CBU_1502; -.
DR   PATRIC; 17931769; VBICoxBur82552_1504.
DR   eggNOG; ENOG4105CWT; Bacteria.
DR   eggNOG; COG1159; LUCA.
DR   HOGENOM; HOG000245596; -.
DR   KO; K03595; -.
DR   OMA; KVAKDWQ; -.
DR   Proteomes; UP000002671; 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-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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; IPR005662; GTP-bd_Era.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_prok-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
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   Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm;
KW   GTP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding.
FT   CHAIN         1    295       GTPase Era.
FT                                /FTId=PRO_0000180010.
FT   DOMAIN        5    172       Era-type G.
FT   DOMAIN      203    279       KH type-2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00367}.
FT   NP_BIND      13     20       GTP. {ECO:0000255|HAMAP-Rule:MF_00367}.
FT   NP_BIND      60     64       GTP. {ECO:0000255|HAMAP-Rule:MF_00367}.
FT   NP_BIND     121    124       GTP. {ECO:0000255|HAMAP-Rule:MF_00367}.
SQ   SEQUENCE   295 AA;  33873 MW;  559AB52D2922119E CRC64;
     MKPTYCGYAA IIGRPNVGKS TLLNQLLEQK ISITSRKPQT TRYQILGVKT FKDIQVIYVD
     TPGLHAGTER TINRYMNRTA RGALRDVDAI VFVIEPHWES QDAWVLDNLK EIETPVFLVI
     NKVDKIKNRA ELLPLIEKVS SLYAFQKITP LSAKTGDQVG TLEQAVHQLM PESPFYFPPE
     QVTDRSDQFM ASEIIREKLM RLLGQEIPYS LAVTLIEFRK EEKIIRISAV IWVEKKSQKG
     IVIGKGGERL KRVGTNARLD MEKWFGKRVF LQLWVKVKSG WADNERLLRE LGFEE
//