IF1_SYNFM
ID IF1_SYNFM Reviewed; 73 AA.
AC A0LIL3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Sfum_1578;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK17265.1; -; Genomic_DNA.
DR RefSeq; WP_011698435.1; NC_008554.1.
DR AlphaFoldDB; A0LIL3; -.
DR SMR; A0LIL3; -.
DR STRING; 335543.Sfum_1578; -.
DR EnsemblBacteria; ABK17265; ABK17265; Sfum_1578.
DR KEGG; sfu:Sfum_1578; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_1_0_7; -.
DR OMA; ECLRSAM; -.
DR OrthoDB; 2066663at2; -.
DR Proteomes; UP000001784; 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..73
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000338942"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ SEQUENCE 73 AA; 8307 MW; 7CE6A4E4D7C7EEF9 CRC64;
MAKEDAIEVE GTVVETLPNA MFRVELPNGH RILAHISGKM RMHFIRILPG DKVTVELSPY
DLNRGRITYR SKS