ID   IF1_MYCSP               Reviewed;          90 AA.
AC   P38037;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075};
OS   Mycoplasma sp.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma;
OC   unclassified Mycoplasma.
OX   NCBI_TaxID=2108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8226662; DOI=10.1128/jb.175.22.7150-7159.1993;
RA   Tan M., Klein R., Grant R., Ganem D., Engel J.N.;
RT   "Cloning and characterization of the RNA polymerase alpha-subunit operon of
RT   Chlamydia trachomatis.";
RL   J. Bacteriol. 175:7150-7159(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8226662, AND CORRECTION OF SPECIES OF ORIGIN.
RA   Tan M., Klein R., Grant R., Ganem D., Engel J.N.;
RL   J. Bacteriol. 177:2607-2607(1995).
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   -!- CAUTION: Was originally thought to originate from Chlamydia
CC       trachomatis. {ECO:0000305|PubMed:8226662}.
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DR   EMBL; L23478; AAA16203.1; -; Genomic_DNA.
DR   AlphaFoldDB; P38037; -.
DR   SMR; P38037; -.
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; Protein biosynthesis; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..90
FT                   /note="Translation initiation factor IF-1"
FT                   /id="PRO_0000095827"
FT   DOMAIN          15..90
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   90 AA;  10559 MW;  DDA2C188F66E98BE CRC64;
     MEKLTYYQEI TFNGKKQKRK KEEVIKMTGK VTKMHSTKNY DVLLENDQEI KAYISGKMSL
     HNIKLIPGDM VDVEISPFNL TLGRIVFRHK