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IF1_MYCTU
ID   IF1_MYCTU               Reviewed;          73 AA.
AC   P9WKK3; L0TCT8; P0A5H5; P45957;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; OrderedLocusNames=Rv3462c;
GN   ORFNames=MCB1222.32c, MTCY13E12.15c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS).
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20132820; DOI=10.1016/j.febslet.2010.01.051;
RA   Hatzopoulos G.N., Mueller-Dieckmann J.;
RT   "Structure of translation initiation factor 1 from Mycobacterium
RT   tuberculosis and inferred binding to the 30S ribosomal subunit.";
RL   FEBS Lett. 584:1011-1015(2010).
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; AL123456; CCP46284.1; -; Genomic_DNA.
DR   PIR; C70566; C70566.
DR   RefSeq; NP_217979.1; NC_000962.3.
DR   RefSeq; WP_003418601.1; NZ_NVQJ01000091.1.
DR   PDB; 3I4O; X-ray; 1.47 A; A/B=1-73.
DR   PDBsum; 3I4O; -.
DR   AlphaFoldDB; P9WKK3; -.
DR   SMR; P9WKK3; -.
DR   STRING; 83332.Rv3462c; -.
DR   PaxDb; P9WKK3; -.
DR   DNASU; 887325; -.
DR   GeneID; 64259827; -.
DR   GeneID; 66969202; -.
DR   GeneID; 887325; -.
DR   KEGG; mtu:Rv3462c; -.
DR   TubercuList; Rv3462c; -.
DR   eggNOG; COG0361; Bacteria.
DR   OMA; AHVSGKM; -.
DR   PhylomeDB; P9WKK3; -.
DR   PRO; PR:P9WKK3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
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; IPR004368; TIF_IF1.
DR   PANTHER; PTHR33370; PTHR33370; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00008; infA; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding; rRNA-binding.
FT   CHAIN           1..73
FT                   /note="Translation initiation factor IF-1"
FT                   /id="PRO_0000095828"
FT   DOMAIN          1..73
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT   STRAND          8..18
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   HELIX           39..43
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:3I4O"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:3I4O"
SQ   SEQUENCE   73 AA;  8489 MW;  70CEB2A79E874448 CRC64;
     MAKKDGAIEV EGRVVEPLPN AMFRIELENG HKVLAHISGK MRQHYIRILP EDRVVVELSP
     YDLSRGRIVY RYK
 
 
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