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Database: UniProt
Entry: A0A1E3RWN2_9MYCO
LinkDB: A0A1E3RWN2_9MYCO
Original site: A0A1E3RWN2_9MYCO 
ID   A0A1E3RWN2_9MYCO        Unreviewed;       303 AA.
AC   A0A1E3RWN2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=GTPase Era {ECO:0000256|ARBA:ARBA00020484, ECO:0000256|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000256|HAMAP-Rule:MF_00367};
GN   ORFNames=BHQ17_09860 {ECO:0000313|EMBL:ODQ94260.1};
OS   Mycolicibacterium holsaticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=152142 {ECO:0000313|EMBL:ODQ94260.1, ECO:0000313|Proteomes:UP000094243};
RN   [1] {ECO:0000313|Proteomes:UP000094243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M7 {ECO:0000313|Proteomes:UP000094243};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits GTPase activity. Binds RNA but is probably not
CC       involved in ribosome assembly in mycobacteria. {ECO:0000256|HAMAP-
CC       Rule:MF_00367}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000256|HAMAP-Rule:MF_00367}.
CC       Secreted, cell wall {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Era GTPase family. {ECO:0000256|ARBA:ARBA00007921,
CC       ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|PROSITE-ProRule:PRU01050,
CC       ECO:0000256|RuleBase:RU003761}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODQ94260.1}.
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DR   EMBL; MIGZ01000045; ODQ94260.1; -; Genomic_DNA.
DR   RefSeq; WP_069405047.1; NZ_MIGZ01000045.1.
DR   AlphaFoldDB; A0A1E3RWN2; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000094243; Unassembled WGS sequence.
DR   GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; 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   PRINTS; PR00326; GTP1OBG.
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 wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|HAMAP-Rule:MF_00367};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00367};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00367}; Reference proteome {ECO:0000313|Proteomes:UP000094243};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00367};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00367}.
FT   DOMAIN          5..175
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51713"
FT   DOMAIN          206..289
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          13..20
FT                   /note="G1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          39..43
FT                   /note="G2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          60..63
FT                   /note="G3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          124..127
FT                   /note="G4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          154..156
FT                   /note="G5"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   BINDING         13..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         60..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   303 AA;  33019 MW;  32DF62714B6A2E9E CRC64;
     MTDFRSGFVC FVGRPNTGKS TLTNALVGAK VAITSNRPQT TRHTIRGIVH RDDFQIILVD
     TPGLHRPRTL LGQRLNDLVK DTYSQVDVIG LCIPADERIG PGDRWICEQI RAVAPNTMLI
     AVVTKIDKVA KDRVAAQLVA VSDLVGPDTE IVPVSATTGE NLGVLTDVLA AQLPPGPAFY
     PDGELTDEPE ETLMAELIRE AALEGVRDEL PHSLAVVIEE VSRREGRSPE QGDLVDVRAN
     LFVERDSQKG IVIGKGGARL REVGTAARTS IEKLLGTKVF LDLRVKVAKN WQRDPKQLGR
     LGF
//
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