ID A0A2N6PL17_9MICO Unreviewed; 313 AA.
AC A0A2N6PL17;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CJ198_02300 {ECO:0000313|EMBL:PMB99373.1};
OS Brevibacterium luteolum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=199591 {ECO:0000313|EMBL:PMB99373.1, ECO:0000313|Proteomes:UP000235703};
RN [1] {ECO:0000313|EMBL:PMB99373.1, ECO:0000313|Proteomes:UP000235703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0680 {ECO:0000313|EMBL:PMB99373.1,
RC ECO:0000313|Proteomes:UP000235703};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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:0000256|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367}. Cell
CC membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC {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:PMB99373.1}.
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DR EMBL; PNFZ01000001; PMB99373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6PL17; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000235703; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; 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 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 membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00367}; Membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00367}; Reference proteome {ECO:0000313|Proteomes:UP000235703};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00367};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00367}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00367}.
FT DOMAIN 14..183
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT DOMAIN 214..296
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 22..29
FT /note="G1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 48..52
FT /note="G2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 69..72
FT /note="G3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 133..136
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 162..164
FT /note="G5"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ SEQUENCE 313 AA; 34560 MW; 69068B8387EF574C CRC64;
MTDLFRTDLP EGYRAGFACL VGRPNTGKST LTNALVGSKI AITSAKPQTT RHTIRGIVHR
DDHQLVLVDT PGLHRPRTLL GARLNDLVAA TLSEVDVIGF CLPANERIGP GDRYIAEQLQ
MVSGRTPVVA LVTKTDLVDR ERLTEALIAV EQLGDFADIV PVSARDGYQV DTVDAVLAKH
LPESPPLYPD GEITDEPETV LVAELVREAA LEGVRDELPH SLAVQVEEMR PREDRPEDKP
LWDVHVNLFV ERPSQKAIVI GRKGARLKEI GMTARKNIEA ILGTSIYLDL HVKVAKDWQR
DPKQLGRLGF DFS
//
