IF1_BRUA2
ID IF1_BRUA2 Reviewed; 72 AA.
AC Q2YPC1; P62922; Q57FA2; Q8YF56; Q9ACA6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=BAB1_0282;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=11705955; DOI=10.1128/iai.69.12.7736-7742.2001;
RA Eskra L., Canavessi A., Carey M., Splitter G.A.;
RT "Brucella abortus genes identified following constitutive growth and
RT macrophage infection.";
RL Infect. Immun. 69:7736-7742(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AF288531; AAK11548.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ10238.1; -; Genomic_DNA.
DR RefSeq; WP_002965531.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YPC1; -.
DR SMR; Q2YPC1; -.
DR STRING; 359391.BAB1_0282; -.
DR EnsemblBacteria; CAJ10238; CAJ10238; BAB1_0282.
DR GeneID; 61316487; -.
DR KEGG; bmf:BAB1_0282; -.
DR PATRIC; fig|359391.11.peg.1701; -.
DR HOGENOM; CLU_151267_1_0_5; -.
DR OMA; AHVSGKM; -.
DR Proteomes; UP000002719; 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 2: Evidence at transcript level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..72
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000095753"
FT DOMAIN 1..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
SQ SEQUENCE 72 AA; 8372 MW; 67D1320EB09AE093 CRC64;
MAKEEVLEFP GVVTELLPNA MFRVKLENEH EIIAHTAGRM RKNRIRVLAG DKVLVEMTPY
DLTKGRITYR FK
