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RL9_MYCS2
ID   RL9_MYCS2               Reviewed;         151 AA.
AC   A0R7F6; I7GG97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503};
GN   OrderedLocusNames=MSMEG_6894, MSMEI_6710;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00503}.
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DR   EMBL; CP000480; ABK76149.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP43136.1; -; Genomic_DNA.
DR   RefSeq; WP_003898318.1; NZ_SIJM01000001.1.
DR   RefSeq; YP_891094.1; NC_008596.1.
DR   PDB; 5O60; EM; 3.20 A; H=1-151.
DR   PDB; 5O61; EM; 3.31 A; H=1-151.
DR   PDB; 5XYM; EM; 3.08 A; H=1-151.
DR   PDB; 5ZEB; EM; 3.40 A; H=1-151.
DR   PDB; 5ZEP; EM; 3.40 A; H=1-151.
DR   PDB; 5ZET; EM; 3.20 A; H=1-151.
DR   PDB; 6DZI; EM; 3.46 A; H=1-151.
DR   PDB; 6DZP; EM; 3.42 A; H=1-151.
DR   PDBsum; 5O60; -.
DR   PDBsum; 5O61; -.
DR   PDBsum; 5XYM; -.
DR   PDBsum; 5ZEB; -.
DR   PDBsum; 5ZEP; -.
DR   PDBsum; 5ZET; -.
DR   PDBsum; 6DZI; -.
DR   PDBsum; 6DZP; -.
DR   AlphaFoldDB; A0R7F6; -.
DR   SMR; A0R7F6; -.
DR   IntAct; A0R7F6; 3.
DR   STRING; 246196.MSMEI_6710; -.
DR   PRIDE; A0R7F6; -.
DR   EnsemblBacteria; ABK76149; ABK76149; MSMEG_6894.
DR   EnsemblBacteria; AFP43136; AFP43136; MSMEI_6710.
DR   GeneID; 66738148; -.
DR   KEGG; msg:MSMEI_6710; -.
DR   KEGG; msm:MSMEG_6894; -.
DR   PATRIC; fig|246196.19.peg.6715; -.
DR   eggNOG; COG0359; Bacteria.
DR   OMA; MKIILTH; -.
DR   OrthoDB; 1959318at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.430.100; -; 1.
DR   Gene3D; 3.40.5.10; -; 1.
DR   HAMAP; MF_00503; Ribosomal_L9; 1.
DR   InterPro; IPR000244; Ribosomal_L9.
DR   InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_L9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_L9_C.
DR   InterPro; IPR036791; Ribosomal_L9_C_sf.
DR   InterPro; IPR020070; Ribosomal_L9_N.
DR   InterPro; IPR036935; Ribosomal_L9_N_sf.
DR   PANTHER; PTHR21368; PTHR21368; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SUPFAM; SSF55653; SSF55653; 1.
DR   SUPFAM; SSF55658; SSF55658; 1.
DR   TIGRFAMs; TIGR00158; L9; 1.
DR   PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..151
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_1000014811"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:5XYM"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   HELIX           23..28
FT                   /evidence="ECO:0007829|PDB:5XYM"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:5XYM"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:5XYM"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   HELIX           63..72
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:5O60"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   HELIX           98..106
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          125..134
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:5ZET"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:5ZET"
SQ   SEQUENCE   151 AA;  15923 MW;  CA4F4ABB3E45F66B CRC64;
     MKLILTAEVE HLGAAGDTVE VKDGYGRNYL LPRGLAIVAS RGAERQAEEI RRARESKVIR
     DIEHANELKT ALEGLGDVTL SVNAAGDTGK LFGSVTAADV VNAIKKAGGP NLDKRTVQLA
     KAHIKSVGTH PVTVKLHTGV EAKVSLNVVA Q
 
 
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