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Database: UniProt
Entry: H2J781_MARPK
LinkDB: H2J781_MARPK
Original site: H2J781_MARPK 
ID   H2J781_MARPK            Unreviewed;        83 AA.
AC   H2J781;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=Marpi_0857 {ECO:0000313|EMBL:AEX85273.1};
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Marinitoga.
OX   NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85273.1, ECO:0000313|Proteomes:UP000007161};
RN   [1] {ECO:0000313|EMBL:AEX85273.1, ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RX   PubMed=23045491; DOI=10.1128/JB.01430-12;
RA   Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA   Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT   "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT   Bacterium Marinitoga piezophila KA3.";
RL   J. Bacteriol. 194:5974-5975(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) 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; CP003257; AEX85273.1; -; Genomic_DNA.
DR   RefSeq; WP_014296345.1; NC_016751.1.
DR   AlphaFoldDB; H2J781; -.
DR   STRING; 443254.Marpi_0857; -.
DR   KEGG; mpz:Marpi_0857; -.
DR   eggNOG; COG0361; Bacteria.
DR   HOGENOM; CLU_151267_0_1_0; -.
DR   OrthoDB; 9803250at2; -.
DR   Proteomes; UP000007161; 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; 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   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:UP000007161};
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   83 AA;  9579 MW;  A0096BA0BAE52745 CRC64;
     MAKKDDVIVM EGHIVESLPN ATFRVELDNG HKILAHISGK MRKNFIRLVP GDRVIVEVSI
     YDLNRGRIIR RERIKKNPSS EEE
//
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