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P12735 (RL4_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L4
Alternative name(s):
Hl6
Hmal4
Gene names
Name:rpl4
Ordered Locus Names:rrnAC1610
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly By similarity. HAMAP-Rule MF_01328_A

Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit. HAMAP-Rule MF_01328_A

Forms part of the polypeptide exit tunnel, in which it helps forms a bend with protein L22. Contacts the macrolide antibiotic spiramycin in the polypeptide exit tunnel. HAMAP-Rule MF_01328_A

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with proteins L18e, L24 and L37e. Has been cross-linked to L18e. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the ribosomal protein L4P family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24624650S ribosomal protein L4 HAMAP-Rule MF_01328_A
PRO_0000129329

Experimental info

Sequence conflict1541V → K AA sequence Ref.3

Secondary structure

................................................ 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12735 [UniParc].

Last modified January 4, 2005. Version 4.
Checksum: 4BCA2FE20EE24EDF

FASTA24626,420
        10         20         30         40         50         60 
MQATIYDLDG NTDGEVDLPD VFETPVRSDL IGKAVRAAQA NRKQDYGSDE YAGLRTPAES 

        70         80         90        100        110        120 
FGSGRGQAHV PKQDGRARRV PQAVKGRSAH PPKTEKDRSL DLNDKERQLA VRSALAATAD 

       130        140        150        160        170        180 
ADLVADRGHE FDRDEVPVVV SDDFEDLVKT QEVVSLLEAL DVHADIDRAD ETKIKAGQGS 

       190        200        210        220        230        240 
ARGRKYRRPA SILFVTSDEP STAARNLAGA DVATASEVNT EDLAPGGAPG RLTVFTESAL 


AEVAER 

« Hide

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui."
Arndt E., Kroemer W., Hatakeyama T.
J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]"Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane."
Walsh M.J., McDougall J., Wittmann-Liebold B.
Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-28 AND 153-181.
[4]"Localization of proteins HL29 and HL31 from Haloarcula marismortui within the 50 S ribosomal subunit by chemical crosslinking."
Bergmann U., Wittmann-Liebold B.
J. Mol. Biol. 232:693-700(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-47; 86-117 AND 176-200, CROSS-LINKING TO L18E.
[5]"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution."
Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.
Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[6]"The structural basis of ribosome activity in peptide bond synthesis."
Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.
Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[7]"A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits."
Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.
Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[8]"The kink-turn: a new RNA secondary structure motif."
Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.
EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[9]"The structures of four macrolide antibiotics bound to the large ribosomal subunit."
Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.
Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[10]"Structural insights into peptide bond formation."
Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[11]"Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit."
Hansen J.L., Moore P.B., Steitz T.A.
J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[12]"Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit."
Schmeing T.M., Moore P.B., Steitz T.A.
RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
[13]"Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
Gabdulkhakov A., Nikonov S., Garber M.
Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05222 Genomic DNA. Translation: AAA86860.1.
AY596297 Genomic DNA. Translation: AAV46527.1.
PIRR5HS6H. D35063.
RefSeqYP_136233.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40C1-246[»]
1JJ2X-ray2.40C1-246[»]
1K73X-ray3.01E1-246[»]
1K8AX-ray3.00E1-246[»]
1K9MX-ray3.00E1-246[»]
1KC8X-ray3.01E1-246[»]
1KD1X-ray3.00E1-246[»]
1KQSX-ray3.10C1-246[»]
1M1KX-ray3.20E1-246[»]
1M90X-ray2.80E1-246[»]
1ML5electron microscopy14.00f1-246[»]
1N8RX-ray3.00E1-246[»]
1NJIX-ray3.00E1-246[»]
1Q7YX-ray3.20E1-246[»]
1Q81X-ray2.95E1-246[»]
1Q82X-ray2.98E1-246[»]
1Q86X-ray3.00E1-246[»]
1QVFX-ray3.10C1-246[»]
1QVGX-ray2.90C1-246[»]
1S72X-ray2.40C1-246[»]
1VQ4X-ray2.70C1-246[»]
1VQ5X-ray2.60C1-246[»]
1VQ6X-ray2.70C1-246[»]
1VQ7X-ray2.50C1-246[»]
1VQ8X-ray2.20C1-246[»]
1VQ9X-ray2.40C1-246[»]
1VQKX-ray2.30C1-246[»]
1VQLX-ray2.30C1-246[»]
1VQMX-ray2.30C1-246[»]
1VQNX-ray2.40C1-246[»]
1VQOX-ray2.20C1-246[»]
1VQPX-ray2.25C1-246[»]
1W2BX-ray3.50C1-246[»]
1YHQX-ray2.40C1-246[»]
1YI2X-ray2.65C1-246[»]
1YIJX-ray2.60C1-246[»]
1YITX-ray2.80C1-246[»]
1YJ9X-ray2.90C1-246[»]
1YJNX-ray3.00C1-246[»]
1YJWX-ray2.90C1-246[»]
2B66X-ray5.90F1-246[»]
2B9NX-ray6.76F1-246[»]
2B9PX-ray6.46F1-246[»]
2OTJX-ray2.90C1-246[»]
2OTLX-ray2.70C1-246[»]
2QA4X-ray3.00C1-246[»]
2QEXX-ray2.90C1-246[»]
3CC2X-ray2.40C1-246[»]
3CC4X-ray2.70C1-246[»]
3CC7X-ray2.70C1-246[»]
3CCEX-ray2.75C1-246[»]
3CCJX-ray2.70C1-246[»]
3CCLX-ray2.90C1-246[»]
3CCMX-ray2.55C1-246[»]
3CCQX-ray2.90C1-246[»]
3CCRX-ray3.00C1-246[»]
3CCSX-ray2.95C1-246[»]
3CCUX-ray2.80C1-246[»]
3CCVX-ray2.90C1-246[»]
3CD6X-ray2.75C1-246[»]
3CMAX-ray2.80C1-246[»]
3CMEX-ray2.95C1-246[»]
3CPWX-ray2.70C1-246[»]
3CXCX-ray3.00C1-246[»]
3G4SX-ray3.20C1-246[»]
3G6EX-ray2.70C1-246[»]
3G71X-ray2.85C1-246[»]
3I55X-ray3.11C1-246[»]
3I56X-ray2.90C1-246[»]
3OW2X-ray2.70C1-246[»]
4ADXelectron microscopy6.60C1-246[»]
4HUBX-ray2.40C1-246[»]
ProteinModelPortalP12735.
SMRP12735. Positions 1-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46527; AAV46527; rrnAC1610.
GeneID3128386.
KEGGhma:rrnAC1610.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0088.
HOGENOMHOG000107332.
KOK02930.
OMAVADRGHE.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1466-MONOMER.

Family and domain databases

Gene3D3.40.1370.10. 1 hit.
HAMAPMF_01328_A. Ribosomal_L4_A.
InterProIPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
IPR019970. Ribosomall_L4.
[Graphical view]
PfamPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMSSF52166. SSF52166. 1 hit.
TIGRFAMsTIGR03672. rpl4p_arch. 1 hit.
PROSITEPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12735.

Entry information

Entry nameRL4_HALMA
AccessionPrimary (citable) accession number: P12735
Secondary accession number(s): Q5V1S5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references