ID IF11_POLAQ Reviewed; 72 AA.
AC A4SUY2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Translation initiation factor IF-1 1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA1 {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Pnuc_0074;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP33296.1; -; Genomic_DNA.
DR RefSeq; WP_011901921.1; NC_009379.1.
DR AlphaFoldDB; A4SUY2; -.
DR SMR; A4SUY2; -.
DR GeneID; 31480420; -.
DR KEGG; pnu:Pnuc_0074; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_1_0_4; -.
DR Proteomes; UP000000231; 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; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00008; infA; 1.
DR PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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 1"
FT /id="PRO_0000338884"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ SEQUENCE 72 AA; 8287 MW; BC550BE49B81B640 CRC64;
MSKDDVIQMA GEVVENLPNA MFRVKLENGH VFLGHISGKM RMHYIRILPG DKVTVEMTPY
DLTRARIIFR AK
//
