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IF3_CAMJR
ID   IF3_CAMJR               Reviewed;         172 AA.
AC   Q5HWW2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN   Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=CJE0200;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW34794.1; -; Genomic_DNA.
DR   RefSeq; WP_002851726.1; NC_003912.7.
DR   PDB; 2M71; NMR; -; A=83-172.
DR   PDBsum; 2M71; -.
DR   AlphaFoldDB; Q5HWW2; -.
DR   BMRB; Q5HWW2; -.
DR   SMR; Q5HWW2; -.
DR   KEGG; cjr:CJE0200; -.
DR   HOGENOM; CLU_054919_3_2_7; -.
DR   OMA; RNMIMFL; -.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..172
FT                   /note="Translation initiation factor IF-3"
FT                   /id="PRO_0000177499"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   HELIX           98..113
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   HELIX           133..146
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:2M71"
FT   STRAND          160..169
FT                   /evidence="ECO:0007829|PDB:2M71"
SQ   SEQUENCE   172 AA;  19781 MW;  E336083CDC1B87C7 CRC64;
     MSKEKEVLLN EEIRADEIRC VGDDGKVYGI ISSDEALEIA NRLGLDLVMI AADAKPPVCK
     IMDYGKFRYQ QEKKQKEAKK KQKVIDIKEI KLSVKIAQND INYKVKHALE FLEQGKHVRF
     RVFLKGREMA TPEAGVALLE KIWTMIENEA NRDKEPNFEG RYVNMLVTPK KA
 
 
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