IF1_SPHAL
ID IF1_SPHAL Reviewed; 72 AA.
AC Q1GRU4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Sala_1916;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000356; ABF53628.1; -; Genomic_DNA.
DR RefSeq; WP_010162480.1; NC_008048.1.
DR AlphaFoldDB; Q1GRU4; -.
DR SMR; Q1GRU4; -.
DR STRING; 317655.Sala_1916; -.
DR EnsemblBacteria; ABF53628; ABF53628; Sala_1916.
DR KEGG; sal:Sala_1916; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_1_0_5; -.
DR OMA; AHVSGKM; -.
DR OrthoDB; 2066663at2; -.
DR Proteomes; UP000006578; Chromosome.
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; IPR022967; S1_dom.
DR InterPro; IPR004368; TIF_IF1.
DR PANTHER; PTHR33370; PTHR33370; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00316; S1; 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; Protein biosynthesis; Reference proteome;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..72
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000263875"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ SEQUENCE 72 AA; 8411 MW; 8CBC4AA36CCFA599 CRC64;
MAKEELLEMR GQVVELLPNA MFRVKLENDH EILGHTAGKM RKNRIRVLVG DEVLVELTPY
DLTKGRITYR FK