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Protein

50S ribosomal protein L4

Gene

rpl4

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity
Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1466-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L4
Alternative name(s):
Hl6
Hmal4
Gene namesi
Name:rpl4
Ordered Locus Names:rrnAC1610
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24624650S ribosomal protein L4PRO_0000129329Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts weakly with proteins L18e, L24 and L37e. Has been cross-linked to L18e.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1610.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni8 – 103Combined sources
Beta strandi12 – 176Combined sources
Helixi20 – 234Combined sources
Helixi28 – 4114Combined sources
Turni50 – 545Combined sources
Beta strandi63 – 664Combined sources
Beta strandi71 – 733Combined sources
Beta strandi94 – 963Combined sources
Helixi104 – 11714Combined sources
Helixi121 – 1277Combined sources
Beta strandi137 – 1404Combined sources
Helixi142 – 1465Combined sources
Helixi150 – 15910Combined sources
Helixi164 – 1685Combined sources
Helixi178 – 1825Combined sources
Beta strandi193 – 1997Combined sources
Turni202 – 2065Combined sources
Beta strandi211 – 2144Combined sources
Turni215 – 2173Combined sources
Helixi220 – 2234Combined sources
Helixi225 – 2273Combined sources
Beta strandi233 – 2364Combined sources
Helixi237 – 2426Combined sources
Helixi243 – 2453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
4V4RX-ray5.90F1-246[»]
4V4SX-ray6.76F1-246[»]
4V4TX-ray6.46F1-246[»]
4V9FX-ray2.40C1-246[»]
ProteinModelPortaliP12735.
SMRiP12735. Positions 1-246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12735.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000107332.
KOiK02930.
OMAiRSAHPPK.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_A. Ribosomal_L4_A.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
IPR019970. Ribosomall_L4.
[Graphical view]
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03672. rpl4p_arch. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQATIYDLDG NTDGEVDLPD VFETPVRSDL IGKAVRAAQA NRKQDYGSDE
60 70 80 90 100
YAGLRTPAES FGSGRGQAHV PKQDGRARRV PQAVKGRSAH PPKTEKDRSL
110 120 130 140 150
DLNDKERQLA VRSALAATAD ADLVADRGHE FDRDEVPVVV SDDFEDLVKT
160 170 180 190 200
QEVVSLLEAL DVHADIDRAD ETKIKAGQGS ARGRKYRRPA SILFVTSDEP
210 220 230 240
STAARNLAGA DVATASEVNT EDLAPGGAPG RLTVFTESAL AEVAER
Length:246
Mass (Da):26,420
Last modified:January 4, 2005 - v4
Checksum:i4BCA2FE20EE24EDF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541V → K AA sequence (PubMed:3196689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86860.1.
AY596297 Genomic DNA. Translation: AAV46527.1.
PIRiD35063. R5HS6H.
RefSeqiWP_004957420.1. NC_006396.1.
YP_136233.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46527; AAV46527; rrnAC1610.
GeneIDi3128386.
KEGGihma:rrnAC1610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86860.1.
AY596297 Genomic DNA. Translation: AAV46527.1.
PIRiD35063. R5HS6H.
RefSeqiWP_004957420.1. NC_006396.1.
YP_136233.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
4V4RX-ray5.90F1-246[»]
4V4SX-ray6.76F1-246[»]
4V4TX-ray6.46F1-246[»]
4V9FX-ray2.40C1-246[»]
ProteinModelPortaliP12735.
SMRiP12735. Positions 1-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46527; AAV46527; rrnAC1610.
GeneIDi3128386.
KEGGihma:rrnAC1610.

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000107332.
KOiK02930.
OMAiRSAHPPK.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1466-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP12735.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_A. Ribosomal_L4_A.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
IPR019970. Ribosomall_L4.
[Graphical view]
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03672. rpl4p_arch. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiRL4_HALMA
AccessioniPrimary (citable) accession number: P12735
Secondary accession number(s): Q5V1S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 4, 2005
Last modified: July 22, 2015
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.