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Database: UniProt
Entry: A0A368X780_9BACI
LinkDB: A0A368X780_9BACI
Original site: A0A368X780_9BACI 
ID   A0A368X780_9BACI        Unreviewed;        72 AA.
AC   A0A368X780;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075};
GN   ORFNames=DFR57_11725 {ECO:0000313|EMBL:RCW63549.1};
OS   Saliterribacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX   NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW63549.1, ECO:0000313|Proteomes:UP000252585};
RN   [1] {ECO:0000313|EMBL:RCW63549.1, ECO:0000313|Proteomes:UP000252585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW63549.1,
RC   ECO:0000313|Proteomes:UP000252585};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000256|ARBA:ARBA00010939,
CC       ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCW63549.1}.
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DR   EMBL; QPJJ01000017; RCW63549.1; -; Genomic_DNA.
DR   RefSeq; WP_058305710.1; NZ_QPJJ01000017.1.
DR   AlphaFoldDB; A0A368X780; -.
DR   OrthoDB; 9803250at2; -.
DR   Proteomes; UP000252585; Unassembled WGS sequence.
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; Nucleic acid-binding proteins; 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; IPR003029; S1_domain.
DR   InterPro; IPR004368; TIF_IF1.
DR   NCBIfam; TIGR00008; infA; 1.
DR   PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00075}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00075}; Reference proteome {ECO:0000313|Proteomes:UP000252585};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   72 AA;  8168 MW;  57D25AA6221878DE CRC64;
     MAKDDAIEVE GTVIDTLPNA QFKVELENGH TVLAHVSGKI RMHFIRILPG DKVTVELSPY
     DLTRGRITYR YK
//
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