ERA_LISW6
ID ERA_LISW6 Reviewed; 301 AA.
AC A0AIR3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=lwe1477;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_00367}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00367}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00367, ECO:0000255|PROSITE-ProRule:PRU01050}.
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DR EMBL; AM263198; CAK20895.1; -; Genomic_DNA.
DR RefSeq; WP_011702270.1; NC_008555.1.
DR AlphaFoldDB; A0AIR3; -.
DR SMR; A0AIR3; -.
DR STRING; 386043.lwe1477; -.
DR EnsemblBacteria; CAK20895; CAK20895; lwe1477.
DR GeneID; 61189353; -.
DR KEGG; lwe:lwe1477; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_9; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 984717at2; -.
DR Proteomes; UP000000779; 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-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 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 3: Inferred from homology;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..301
FT /note="GTPase Era"
FT /id="PRO_1000079706"
FT DOMAIN 6..173
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 204..282
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 40..44
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 61..64
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 123..126
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 152..154
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 301 AA; 34489 MW; 7231EC6984D813D3 CRC64;
MSEPFKSGFV AIVGRPNVGK STLLNHIIGQ KIAIMSDKAQ TTRNKVQGVY TTDESQIIFI
DTPGIHKPKH KLGDFMVKIA LNTFQEVDLI YFVIDASTGF GRGDEFIIEK LKNVQTPVFL
LINKIDLISP EDLFKLIEQY RELLDFEEII PISALQGNNV PNLLEQTNAN LEIGPMYYPK
DQITDHPERF IISELIREQV LQLTREEVPH SVAVVIEGIE KNPKTEKLTI NATIIVERST
QKGIIIGKQG QMLKQIGMRA RKEIESLLGS KVFLEIWVKV QKNWRDKEHY LHDYGFDREE
Y