ERA_MYCTU
ID ERA_MYCTU Reviewed; 300 AA.
AC P9WNK9; L0TC41; O05834; P0A562;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=GTPase Era;
GN Name=era; OrderedLocusNames=Rv2364c; ORFNames=MTCY27.16;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A GTPASE, MUTAGENESIS OF ASP-87, AND GTP-BINDING.
RC STRAIN=H37Rv;
RX PubMed=22578863; DOI=10.1016/j.enzmictec.2007.08.008;
RA Meena L.S., Chopra P., Bedwal R.S., Singh Y.;
RT "Cloning and characterization of GTP-binding proteins of Mycobacterium
RT tuberculosis H37Rv.";
RL Enzyme Microb. Technol. 42:138-144(2008).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20705052; DOI=10.1016/j.bbrc.2010.08.023;
RA Han J.S., Lee J.J., Anandan T., Zeng M., Sripathi S., Jahng W.J., Lee S.H.,
RA Suh J.W., Kang C.M.;
RT "Characterization of a chromosomal toxin-antitoxin, Rv1102c-Rv1103c system
RT in Mycobacterium tuberculosis.";
RL Biochem. Biophys. Res. Commun. 400:293-298(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 ECO:0000269|PubMed:22578863}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- INDUCTION: The mRNA can be cleaved by the RV1102c mRNA interferase in
CC E.coli. {ECO:0000269|PubMed:20705052}.
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}.
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DR EMBL; AL123456; CCP45152.1; -; Genomic_DNA.
DR PIR; C70586; C70586.
DR RefSeq; WP_003412224.1; NZ_NVQJ01000029.1.
DR RefSeq; YP_177873.1; NC_000962.3.
DR AlphaFoldDB; P9WNK9; -.
DR SMR; P9WNK9; -.
DR STRING; 83332.Rv2364c; -.
DR iPTMnet; P9WNK9; -.
DR PaxDb; P9WNK9; -.
DR DNASU; 886027; -.
DR GeneID; 45426351; -.
DR GeneID; 886027; -.
DR KEGG; mtu:Rv2364c; -.
DR TubercuList; Rv2364c; -.
DR eggNOG; COG1159; Bacteria.
DR OMA; WAEVDVI; -.
DR PhylomeDB; P9WNK9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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 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 Acetylation; Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..300
FT /note="GTPase Era"
FT /id="PRO_0000180031"
FT DOMAIN 5..176
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 207..286
FT /note="KH type-2"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 39..43
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 60..63
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 155..157
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 60..64
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 MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MUTAGEN 87
FT /note="D->A: No GTPase activity."
FT /evidence="ECO:0000269|PubMed:22578863"
SQ SEQUENCE 300 AA; 32460 MW; 01A5C664C5E9D9D7 CRC64;
MTEFHSGFVC LVGRPNTGKS TLTNALVGAK VAITSTRPQT TRHAIRGIVH SDDFQIILVD
TPGLHRPRTL LGKRLNDLVR ETYAAVDVIG LCIPADEAIG PGDRWIVEQL RSTGPANTTL
VVIVTKIDKV PKEKVVAQLV AVSELVTNAA EIVPVSAMTG DRVDLLIDVL AAALPAGPAY
YPDGELTDEP EEVLMAELIR EAALQGVRDE LPHSLAVVID EVSPREGRDD LIDVHAALYV
ERDSQKGIVI GKGGARLREV GTAARSQIEN LLGTKVYLDL RVKVAKNWQR DPKQLGRLGF
