IF3_HELPJ
ID IF3_HELPJ Reviewed; 203 AA.
AC Q9ZMV2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=jhp_0114;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001439; AAD05693.1; -; Genomic_DNA.
DR PIR; H71972; H71972.
DR RefSeq; WP_000089205.1; NZ_CP011330.1.
DR PDB; 6O6D; X-ray; 1.82 A; A=2-77.
DR PDBsum; 6O6D; -.
DR AlphaFoldDB; Q9ZMV2; -.
DR SMR; Q9ZMV2; -.
DR STRING; 85963.jhp_0114; -.
DR EnsemblBacteria; AAD05693; AAD05693; jhp_0114.
DR KEGG; hpj:jhp_0114; -.
DR PATRIC; fig|85963.30.peg.914; -.
DR eggNOG; COG0290; Bacteria.
DR OMA; RNMIMFL; -.
DR Proteomes; UP000000804; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis.
FT CHAIN 1..203
FT /note="Translation initiation factor IF-3"
FT /id="PRO_0000177526"
FT REGION 172..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:6O6D"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:6O6D"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6O6D"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6O6D"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:6O6D"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6O6D"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:6O6D"
SQ SEQUENCE 203 AA; 23333 MW; E4CBD4C2353E4E32 CRC64;
MSRNEVLLNG DINFKEVRCV GDNGEVYGII SSKEALKIAQ NLGLDLVLIS ASAKPPVCKV
MDYNKFRYQN EKKIKEAKKK QKQIEIKEIK LSTQIAQNDI NYKVKHAREF IESNKHVKFK
VVLKGRESQN SKAGLDVLFR VQTMMQDLAN PEKEPKTEGR FVSWMFVPKA KEAPKNEKKT
KENNPPFNRI NLMKGENHAK NED