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