ID A0A380CIA7_SPOPA Unreviewed; 73 AA.
AC A0A380CIA7;
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 ECO:0000313|EMBL:SUJ21078.1};
GN ORFNames=NCTC4822_03129 {ECO:0000313|EMBL:SUJ21078.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ21078.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ21078.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UGYZ01000002; SUJ21078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380CIA7; -.
DR Proteomes; UP000254519; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00075}; Reference proteome {ECO:0000313|Proteomes:UP000254519};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT DOMAIN 1..73
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 73 AA; 8361 MW; 119E517F15207D8E CRC64;
MMAKDDVIEV EGTVVETLPN AMFKVELENG HTILAHVSGK IRMHFIRILP GDKVTMELSP
YDLTRGRITY RFK
//
