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RL4_ACIB5
ID   RL4_ACIB5               Reviewed;         200 AA.
AC   B7IA38;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=AB57_3529;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC       initially binds near the 5'-end of the 23S rRNA. It is important during
CC       the early stages of 50S assembly. It makes multiple contacts with
CC       different domains of the 23S rRNA in the assembled 50S subunit and
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR   EMBL; CP001182; ACJ42896.1; -; Genomic_DNA.
DR   RefSeq; WP_001050255.1; NC_011586.2.
DR   PDB; 6V39; EM; 3.04 A; E=1-200.
DR   PDB; 6V3A; EM; 2.82 A; E=1-200.
DR   PDB; 6V3B; EM; 2.91 A; E=1-200.
DR   PDB; 6V3D; EM; 2.95 A; E=1-200.
DR   PDB; 7M4V; EM; 2.54 A; E=1-200.
DR   PDB; 7M4W; EM; 2.55 A; E=1-200.
DR   PDB; 7M4X; EM; 2.66 A; E=1-200.
DR   PDB; 7M4Y; EM; 2.50 A; E=1-200.
DR   PDB; 7M4Z; EM; 2.92 A; E=1-200.
DR   PDB; 7RYF; EM; 2.65 A; E=1-200.
DR   PDB; 7RYG; EM; 2.38 A; E=1-200.
DR   PDB; 7RYH; EM; 2.43 A; E=1-200.
DR   PDBsum; 6V39; -.
DR   PDBsum; 6V3A; -.
DR   PDBsum; 6V3B; -.
DR   PDBsum; 6V3D; -.
DR   PDBsum; 7M4V; -.
DR   PDBsum; 7M4W; -.
DR   PDBsum; 7M4X; -.
DR   PDBsum; 7M4Y; -.
DR   PDBsum; 7M4Z; -.
DR   PDBsum; 7RYF; -.
DR   PDBsum; 7RYG; -.
DR   PDBsum; 7RYH; -.
DR   AlphaFoldDB; B7IA38; -.
DR   SMR; B7IA38; -.
DR   IntAct; B7IA38; 2.
DR   GeneID; 66395741; -.
DR   KEGG; abn:AB57_3529; -.
DR   HOGENOM; CLU_041575_5_2_6; -.
DR   OMA; PQVHILE; -.
DR   Proteomes; UP000007094; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03953; rplD_bact; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..200
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000142062"
FT   REGION          42..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           15..18
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           24..37
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           97..114
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           130..139
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          143..151
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           154..161
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           176..181
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:7M4V"
FT   HELIX           189..198
FT                   /evidence="ECO:0007829|PDB:7M4V"
SQ   SEQUENCE   200 AA;  21552 MW;  E71323C1C29B76B7 CRC64;
     MNLKTVSGSA VELSEVAFGR EFNEALVHQV VTAYLAGGRQ GTRAHKSRAD VSGGGKKPFR
     QKGTGRARAG SIRSPIWVGG GKTFAARPQD WSQKVNRKMY RGAMQCILAE LVRQDRLVLV
     EEFAVAAPKT KELLAKLNDL NAARALIVTD AVDENLYLAA RNLPHVDVVD ATAIDPVSLI
     AFDKVVMSVA AAKKIEVELG
 
 
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