ID   IF3_SALPA               Reviewed;         180 AA.
AC   Q5PH88;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=SPA1510;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77443.1; -; Genomic_DNA.
DR   RefSeq; WP_011233062.1; NC_006511.1.
DR   AlphaFoldDB; Q5PH88; -.
DR   SMR; Q5PH88; -.
DR   PRIDE; Q5PH88; -.
DR   EnsemblBacteria; AAV77443; AAV77443; SPA1510.
DR   KEGG; spt:SPA1510; -.
DR   HOGENOM; CLU_054919_3_2_6; -.
DR   OMA; RNMIMFL; -.
DR   Proteomes; UP000008185; 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; IPR019813; Translation_initiation_fac3_CS.
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.
DR   PROSITE; PS00938; IF3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..180
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_1000004563"
SQ   SEQUENCE   180 AA;  20624 MW;  C531BA238CB74F0E CRC64;
     MKGGKRVQTA RPNRINSEIR AQEVRLTGLE GEQLGIVSLR EALEKTEEAG VDLVEISPNA
     EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP GTDEGDYQVK LRSLIRFLEE
     GDKAKITLRF RGREMAHQQI GMEVLNRVKD DLQELAVVES FPTKIEGRQM IMVLAPKKKQ