ID   IF3_PORGI               Reviewed;         201 AA.
AC   Q7MVQ6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=PG_0991;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
CC   -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the
CC       equilibrum between 70S ribosomes and their 50S and 30S subunits in
CC       favor of the free subunits, thus enhancing the availability of 30S
CC       subunits on which protein synthesis initiation begins.
CC       {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00080}.
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DR   EMBL; AE015924; AAQ66114.1; -; Genomic_DNA.
DR   RefSeq; WP_005874110.1; NC_002950.2.
DR   AlphaFoldDB; Q7MVQ6; -.
DR   SMR; Q7MVQ6; -.
DR   STRING; 242619.PG_0991; -.
DR   EnsemblBacteria; AAQ66114; AAQ66114; PG_0991.
DR   KEGG; pgi:PG_0991; -.
DR   eggNOG; COG0290; Bacteria.
DR   HOGENOM; CLU_054919_3_2_10; -.
DR   OMA; RNMIMFL; -.
DR   OrthoDB; 1760144at2; -.
DR   Proteomes; UP000000588; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.20.80; -; 1.
DR   Gene3D; 3.30.110.10; -; 1.
DR   HAMAP; MF_00080; IF_3; 1.
DR   InterPro; IPR036788; T_IF-3_C_sf.
DR   InterPro; IPR036787; T_IF-3_N_sf.
DR   InterPro; IPR001288; Translation_initiation_fac_3.
DR   InterPro; IPR019815; Translation_initiation_fac_3_C.
DR   InterPro; IPR019814; Translation_initiation_fac_3_N.
DR   PANTHER; PTHR10938; PTHR10938; 1.
DR   Pfam; PF00707; IF3_C; 1.
DR   Pfam; PF05198; IF3_N; 1.
DR   SUPFAM; SSF54364; SSF54364; 1.
DR   SUPFAM; SSF55200; SSF55200; 1.
DR   TIGRFAMs; TIGR00168; infC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..201
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_0000177552"
FT   REGION          170..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  23148 MW;  87907AD76858792F CRC64;
     MAIDKTKNQH RINEAIRVKE VRLVGDNVEQ GVYNIQEARR IAESQDLDLV EISPNADPPV
     CRVTDYQKFV YQLKKKAKEQ KAKSVKIVIK EIRFGPQTDD HDYNFKLKHA KEFLQEGSKV
     KAYVFFRGRS ILFKEQGEVL LLRFANDLED FARVEQMPIL EGKRMTIMLT PKSASKKGHT
     PPKTQVEASK QANESAETEE E