IF1_BURTA
ID IF1_BURTA Reviewed; 72 AA.
AC Q2SU48;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=BTH_I3047;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RA Barnwal R., Varani G.;
RT "NMR assignments and structure of translation initiation factor IF-1 from
RT Burkholderia thailandensis E264.";
RL Submitted (JUN-2015) to the PDB data bank.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit
CC to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps
CC modulate mRNA selection, yielding the 30S pre-initiation complex (PIC).
CC Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are
CC released leaving the mature 70S translation initiation complex.
CC {ECO:0000255|HAMAP-Rule:MF_00075}.
CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC any time during PIC assembly. {ECO:0000255|HAMAP-Rule:MF_00075}.
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; CP000086; ABC39541.1; -; Genomic_DNA.
DR RefSeq; WP_004521905.1; NZ_CP008786.1.
DR PDB; 2N3S; NMR; -; A=1-72.
DR PDBsum; 2N3S; -.
DR AlphaFoldDB; Q2SU48; -.
DR SMR; Q2SU48; -.
DR PRIDE; Q2SU48; -.
DR EnsemblBacteria; ABC39541; ABC39541; BTH_I3047.
DR GeneID; 60548068; -.
DR GeneID; 62009766; -.
DR GeneID; 64462478; -.
DR GeneID; 67433089; -.
DR KEGG; bte:BTH_I3047; -.
DR HOGENOM; CLU_151267_1_0_4; -.
DR OMA; ECLRSAM; -.
DR OrthoDB; 2066663at2; -.
DR Proteomes; UP000001930; Chromosome I.
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; IPR022967; S1_dom.
DR InterPro; IPR004368; TIF_IF1.
DR PANTHER; PTHR33370; PTHR33370; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00316; S1; 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 RNA-binding; rRNA-binding.
FT CHAIN 1..72
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000263777"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:2N3S"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2N3S"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2N3S"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2N3S"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2N3S"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2N3S"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2N3S"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:2N3S"
SQ SEQUENCE 72 AA; 8218 MW; 983A496214B869D9 CRC64;
MAKDDVIQMQ GEVIENLPNA TFRVKLENGH VVLGHISGKM RMHYIRILPG DKVTVELTPY
DLSRARIVFR AK