IF13_CUPMC
ID IF13_CUPMC Reviewed; 73 AA.
AC Q1LCU1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-1 3 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA3 {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Rmet_5176;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit
CC to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps
CC modulate mRNA selection, yielding the 30S pre-initiation complex (PIC).
CC Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are
CC released leaving the mature 70S translation initiation complex.
CC {ECO:0000255|HAMAP-Rule:MF_00075}.
CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC any time during PIC assembly. {ECO:0000255|HAMAP-Rule:MF_00075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}.
CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00075}.
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DR EMBL; CP000353; ABF12035.1; -; Genomic_DNA.
DR RefSeq; WP_008646230.1; NC_007974.2.
DR AlphaFoldDB; Q1LCU1; -.
DR SMR; Q1LCU1; -.
DR STRING; 266264.Rmet_5176; -.
DR EnsemblBacteria; ABF12035; ABF12035; Rmet_5176.
DR GeneID; 60824843; -.
DR KEGG; rme:Rmet_5176; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_4_1_4; -.
DR OMA; VLLENDH; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd04451; S1_IF1; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00075; IF_1; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR004368; TIF_IF1.
DR PANTHER; PTHR33370; PTHR33370; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00008; infA; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Plasmid; Protein biosynthesis;
KW Reference proteome; RNA-binding; rRNA-binding.
FT CHAIN 1..73
FT /note="Translation initiation factor IF-1 3"
FT /id="PRO_0000263851"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ SEQUENCE 73 AA; 8472 MW; DA3295E8B832B9C7 CRC64;
MAKEELVEFG GKVSEVLPDN RFRVILENGF EVWAYSSGRL KKNRIRVLAG DRVTLEMSPY
DLTKGRINYR HKS
