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Database: UniProt
Entry: B2A4G0_NATTJ
LinkDB: B2A4G0_NATTJ
Original site: B2A4G0_NATTJ 
ID   B2A4G0_NATTJ            Unreviewed;        85 AA.
AC   B2A4G0;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075};
GN   OrderedLocusNames=Nther_0218 {ECO:0000313|EMBL:ACB83817.1};
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB83817.1, ECO:0000313|Proteomes:UP000001683};
RN   [1] {ECO:0000313|EMBL:ACB83817.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB83817.1, ECO:0000313|Proteomes:UP000001683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC   {ECO:0000313|Proteomes:UP000001683};
RX   PubMed=21642468; DOI=10.1128/JB.05157-11;
RA   Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA   Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA   Kyrpides N., Wiegel J.;
RT   "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT   Natranaerobius thermophilus JW/NM-WN-LF.";
RL   J. Bacteriol. 193:4023-4024(2011).
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; CP001034; ACB83817.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2A4G0; -.
DR   STRING; 457570.Nther_0218; -.
DR   KEGG; nth:Nther_0218; -.
DR   eggNOG; COG0361; Bacteria.
DR   HOGENOM; CLU_151267_1_0_9; -.
DR   InParanoid; B2A4G0; -.
DR   OMA; GKMRMNF; -.
DR   Proteomes; UP000001683; 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; 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:UP000001683};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT   DOMAIN          10..85
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   85 AA;  9894 MW;  0ECB9D23D059DA77 CRC64;
     MISLTKRREE LSYMSKKEAI EVEGTVVEPL PNAMFRVELE NGHKILAHVS GKIRMNYIRI
     LPGDKVKVEL SPYDLSRGRI TYRYK
//
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