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P12733 (RL18E_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. 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 L18e
Alternative name(s):
Hl29
L19
Gene names
Name:rpl18e
Ordered Locus Names:rrnAC0064
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 length116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain II) to which it binds. HAMAP-Rule MF_00329

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with proteins L4 and L15. Has been cross-linked to L4. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the ribosomal protein L18e 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: InterPro

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.5
Chain2 – 11611550S ribosomal protein L18e HAMAP-Rule MF_00329
PRO_0000132787

Secondary structure

................... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12733 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BFACD702AE94474D

FASTA11612,422
        10         20         30         40         50         60 
MSKTNPRLSS LIADLKSAAR SSGGAVWGDV AERLEKPRRT HAEVNLGRIE RYAQEDETVV 

        70         80         90        100        110 
VPGKVLGSGV LQKDVTVAAV DFSGTAETKI DQVGEAVSLE QAIENNPEGS HVRVIR 

« Hide

References

« Hide 'large scale' references
[1]"Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed with genes encoding a tRNA(Leu), the enolase, and a putative membrane protein in the archaebacterium Haloarcula (Halobacterium) marismortui."
Kroemer W.J., Arndt E.
J. Biol. Chem. 266:24573-24579(1991) [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]"Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui."
Hatakeyama T., Kimura M.
Eur. J. Biochem. 172:703-711(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-116.
[4]"The alpha-operon equivalent genome region in the extreme halophilic archaebacterium Haloarcula (Halobacterium) marismortui."
Scholzen T., Arndt E.
J. Biol. Chem. 267:12123-12130(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
[5]"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 2-24.
[6]"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 4-27; 37-39 AND 65-82, CROSS-LINKING TO L4.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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
M76567 Genomic DNA. Translation: AAA73096.1.
AY596297 Genomic DNA. Translation: AAV45144.1.
M87833 Genomic DNA. Translation: AAA73213.1.
PIRR5HSH9. A41715.
RefSeqYP_134850.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40L2-116[»]
1JJ2X-ray2.40N2-116[»]
1K73X-ray3.01P2-116[»]
1K8AX-ray3.00P2-116[»]
1K9MX-ray3.00P2-116[»]
1KC8X-ray3.01P2-116[»]
1KD1X-ray3.00P2-116[»]
1KQSX-ray3.10N2-116[»]
1M1KX-ray3.20P2-116[»]
1M90X-ray2.80P2-116[»]
1N8RX-ray3.00P2-116[»]
1NJIX-ray3.00P2-116[»]
1Q7YX-ray3.20P2-116[»]
1Q81X-ray2.95P2-116[»]
1Q82X-ray2.98P2-116[»]
1Q86X-ray3.00P2-116[»]
1QVFX-ray3.10N2-116[»]
1QVGX-ray2.90N2-116[»]
1S72X-ray2.40O1-116[»]
1VQ4X-ray2.70O1-116[»]
1VQ5X-ray2.60O1-116[»]
1VQ6X-ray2.70O1-116[»]
1VQ7X-ray2.50O1-116[»]
1VQ8X-ray2.20O1-116[»]
1VQ9X-ray2.40O1-116[»]
1VQKX-ray2.30O1-116[»]
1VQLX-ray2.30O1-116[»]
1VQMX-ray2.30O1-116[»]
1VQNX-ray2.40O1-116[»]
1VQOX-ray2.20O1-116[»]
1VQPX-ray2.25O1-116[»]
1W2BX-ray3.50N2-115[»]
1YHQX-ray2.40O1-116[»]
1YI2X-ray2.65O1-116[»]
1YIJX-ray2.60O1-116[»]
1YITX-ray2.80O1-116[»]
1YJ9X-ray2.90O1-116[»]
1YJNX-ray3.00O1-116[»]
1YJWX-ray2.90O1-116[»]
2OTJX-ray2.90O1-116[»]
2OTLX-ray2.70O1-116[»]
2QA4X-ray3.00O1-116[»]
2QEXX-ray2.90O1-116[»]
3CC2X-ray2.40O1-116[»]
3CC4X-ray2.70O1-116[»]
3CC7X-ray2.70O1-116[»]
3CCEX-ray2.75O1-116[»]
3CCJX-ray2.70O1-116[»]
3CCLX-ray2.90O1-116[»]
3CCMX-ray2.55O1-116[»]
3CCQX-ray2.90O1-116[»]
3CCRX-ray3.00O1-116[»]
3CCSX-ray2.95O1-116[»]
3CCUX-ray2.80O1-116[»]
3CCVX-ray2.90O1-116[»]
3CD6X-ray2.75O1-116[»]
3CMAX-ray2.80O1-116[»]
3CMEX-ray2.95O1-116[»]
3CPWX-ray2.70N1-116[»]
3CXCX-ray3.00N2-115[»]
3G4SX-ray3.20O2-116[»]
3G6EX-ray2.70O2-116[»]
3G71X-ray2.85O2-116[»]
3I55X-ray3.11O1-116[»]
3I56X-ray2.90O1-116[»]
3OW2X-ray2.70N2-116[»]
4HUBX-ray2.40O1-116[»]
ProteinModelPortalP12733.
SMRP12733. Positions 2-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC0064.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV45144; AAV45144; rrnAC0064.
GeneID3130533.
KEGGhma:rrnAC0064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1727.
HOGENOMHOG000225300.
KOK02883.
OMANPKGSNV.
ProtClustDBPRK04005.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-60-MONOMER.

Family and domain databases

HAMAPMF_00329. Ribosomal_L18e.
InterProIPR001196. Ribosomal_L15_CS.
IPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR022947. Ribosomal_L18e_arc.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERPTHR10934. PTHR10934. 1 hit.
PfamPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMSSF52080. SSF52080. 1 hit.
PROSITEPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12733.

Entry information

Entry nameRL18E_HALMA
AccessionPrimary (citable) accession number: P12733
Secondary accession number(s): Q5V5Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 111 of the entry and version 2 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