ID   IF1_STRPN               Reviewed;          72 AA.
AC   P65121; Q97SU0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=SP_0232;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS).
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Stogios P.J., Wawrzak Z., Onopriyenko O., Savchenko A., Anderson W.F.;
RT   "Crystal structure of translation initiation factor IF-1 from Streptococcus
RT   pneumoniae TIGR4.";
RL   Submitted (JUN-2014) to the PDB data bank.
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; AE005672; AAK74412.1; -; Genomic_DNA.
DR   PIR; C95027; C95027.
DR   RefSeq; WP_001029883.1; NZ_AKVY01000001.1.
DR   PDB; 4QL5; X-ray; 2.02 A; A/B=1-72.
DR   PDBsum; 4QL5; -.
DR   AlphaFoldDB; P65121; -.
DR   SMR; P65121; -.
DR   STRING; 170187.SP_0232; -.
DR   EnsemblBacteria; AAK74412; AAK74412; SP_0232.
DR   GeneID; 60232747; -.
DR   GeneID; 61537047; -.
DR   GeneID; 64075828; -.
DR   GeneID; 66805438; -.
DR   KEGG; spn:SP_0232; -.
DR   eggNOG; COG0361; Bacteria.
DR   OMA; AHVSGKM; -.
DR   PhylomeDB; P65121; -.
DR   BioCyc; SPNE170187:G1FZB-236-MON; -.
DR   Proteomes; UP000000585; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..72
FT                   /note="Translation initiation factor IF-1"
FT                   /id="PRO_0000095879"
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:4QL5"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:4QL5"
SQ   SEQUENCE   72 AA;  8203 MW;  E4BA760D8186419F CRC64;
     MAKDDVIEVE GKVVDTMPNA MFTVELENGH QILATVSGKI RKNYIRILAG DRVTVEMSPY
     DLTRGRITYR FK