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 01-MAY-2013, entry version 91. DE RecName: Full=GTPase Era; GN Name=era; 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 (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral CC membrane protein (By similarity). 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. CC -!- SIMILARITY: Belongs to the Era/MnmE GTP-binding protein family. CC Era subfamily. CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain. CC -!- SIMILARITY: Contains 1 KH type-2 domain. 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; 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 ProteinModelPortal; P51836; -. DR SMR; P51836; 3-291. DR STRING; 227377.CBU_1502; -. DR EnsemblBacteria; AAO90999; AAO90999; CBU_1502. DR GeneID; 1209412; -. DR KEGG; cbu:CBU_1502; -. DR PATRIC; 17931769; VBICoxBur82552_1504. DR eggNOG; COG1159; -. DR HOGENOM; HOG000245596; -. DR KO; K03595; -. DR OMA; KVAKDWQ; -. DR ProtClustDB; PRK00089; -. DR BioCyc; CBUR227377:GJ7S-1487-MONOMER; -. 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:HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:HAMAP. DR GO; GO:0070181; F:SSU rRNA binding; IEA:HAMAP. DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_00367; GTPase_Era; 1; -. 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; IPR005225; Small_GTP-bd_dom. DR Pfam; PF07650; KH_2; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF54814; KH_prok; 1. DR TIGRFAMs; TIGR00436; era; 1. DR TIGRFAMs; TIGR00231; small_GTP; 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 18 122 G. FT DOMAIN 203 279 KH type-2. FT NP_BIND 13 20 GTP (Potential). FT NP_BIND 60 64 GTP (Potential). FT NP_BIND 121 124 GTP (Potential). 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 //