IF1_THET8
ID IF1_THET8 Reviewed; 72 AA.
AC Q5SHR1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=TTHA1669;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW.
RX PubMed=22515367; DOI=10.3109/10409238.2012.678284;
RA Milon P., Rodnina M.V.;
RT "Kinetic control of translation initiation in bacteria.";
RL Crit. Rev. Biochem. Mol. Biol. 47:334-348(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-72, FUNCTION, INTERACTION WITH
RP S12, SUBUNIT, RIBOSOME-BINDING, AND RRNA-BINDING.
RX PubMed=11228145; DOI=10.1126/science.1057766;
RA Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J.,
RA Hartsch T., Wimberly B.T., Ramakrishnan V.;
RT "Crystal structure of an initiation factor bound to the 30S ribosomal
RT subunit.";
RL Science 291:498-501(2001).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Binds in the vicinity of the A-site
CC (ECO:0000269|PubMed:11228145). Stabilizes the binding of IF-2 and IF-3
CC on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently
CC binds. Helps modulate mRNA selection, yielding the 30S pre-initiation
CC complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2
CC and IF-3 are released leaving the mature 70S translation initiation
CC complex. {ECO:0000255|HAMAP-Rule:MF_00075,
CC ECO:0000269|PubMed:11228145}.
CC -!- SUBUNIT: Binds to the 30S ribosomal subunit, contacting protein S12 and
CC the 16S rRNA (ECO:0000269|PubMed:11228145). Component of the 30S
CC ribosomal translation pre-initiation complex which assembles on the 30S
CC ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-
CC tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
CC {ECO:0000255|HAMAP-Rule:MF_00075, ECO:0000269|PubMed:11228145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}.
CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00075}.
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DR EMBL; AP008226; BAD71492.1; -; Genomic_DNA.
DR RefSeq; WP_008633373.1; NC_006461.1.
DR RefSeq; YP_144935.1; NC_006461.1.
DR PDB; 1HR0; X-ray; 3.20 A; W=2-72.
DR PDB; 5LMN; EM; 3.55 A; W=1-72.
DR PDB; 5LMO; EM; 4.30 A; W=1-72.
DR PDB; 5LMP; EM; 5.35 A; W=1-72.
DR PDB; 5LMQ; EM; 4.20 A; W=1-72.
DR PDB; 5LMR; EM; 4.45 A; W=1-72.
DR PDB; 5LMS; EM; 5.10 A; W=1-72.
DR PDB; 5LMT; EM; 4.15 A; W=1-72.
DR PDB; 5LMV; EM; 4.90 A; W=1-72.
DR PDB; 5ME0; EM; 13.50 A; V=1-72.
DR PDB; 5ME1; EM; 13.50 A; V=1-72.
DR PDBsum; 1HR0; -.
DR PDBsum; 5LMN; -.
DR PDBsum; 5LMO; -.
DR PDBsum; 5LMP; -.
DR PDBsum; 5LMQ; -.
DR PDBsum; 5LMR; -.
DR PDBsum; 5LMS; -.
DR PDBsum; 5LMT; -.
DR PDBsum; 5LMV; -.
DR PDBsum; 5ME0; -.
DR PDBsum; 5ME1; -.
DR AlphaFoldDB; Q5SHR1; -.
DR SMR; Q5SHR1; -.
DR IntAct; Q5SHR1; 23.
DR STRING; 300852.55773051; -.
DR EnsemblBacteria; BAD71492; BAD71492; BAD71492.
DR GeneID; 3168806; -.
DR KEGG; ttj:TTHA1669; -.
DR PATRIC; fig|300852.9.peg.1639; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_1_0_0; -.
DR OMA; AHVSGKM; -.
DR PhylomeDB; Q5SHR1; -.
DR EvolutionaryTrace; Q5SHR1; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd04451; S1_IF1; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00075; IF_1; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR004368; TIF_IF1.
DR PANTHER; PTHR33370; PTHR33370; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00008; infA; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding; rRNA-binding.
FT CHAIN 1..72
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000095893"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1HR0"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1HR0"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1HR0"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1HR0"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1HR0"
SQ SEQUENCE 72 AA; 8234 MW; 981E63B61223DDFC CRC64;
MAKEKDTIRT EGVVTEALPN ATFRVKLDSG PEILAYISGK MRMHYIRILP GDRVVVEITP
YDPTRGRIVY RK
