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P14123 (RL18_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 113. 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 L18P
Alternative name(s):
Hl12
Hmal18
Gene names
Name:rpl18p
Ordered Locus Names:rrnAC1593
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 length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, where it forms part of the central protuberance and stabilizes the orientation of adjacent RNA domains. HAMAP-Rule MF_01337_A

Subunit structure

Part of the 50S ribosomal subunit. Interacts with proteins L5 and L21e, and attaches the 5S rRNA to the 23S rRNA. Has been cross-linked to L21e. 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 L18P 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_function5S rRNA binding

Inferred from electronic annotation. Source: InterPro

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
Chain2 – 18718650S ribosomal protein L18P HAMAP-Rule MF_01337_A
PRO_0000131400

Experimental info

Sequence conflict181R → A AA sequence Ref.3

Secondary structure

.................................... 187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14123 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 60E9AF3CB64E7CA5

FASTA18720,614
        10         20         30         40         50         60 
MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT LGPNGDDTLA 

        70         80         90        100        110        120 
SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE AVLDIGLNSP TPGSKVFAIQ 

       130        140        150        160        170        180 
EGAIDAGLDI PHNDDVLADW QRTRGAHIAE YDEQLEEPLY SGDFDAADLP EHFDELRETL 


LDGDIEL 

« Hide

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui."
Scholzen T., Arndt E.
Mol. Gen. Genet. 228:70-80(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]"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 2-25.
[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: CROSS-LINKING TO L21E.
[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
X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.
PIRR5HS18. S16541.
RefSeqYP_136217.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40K2-187[»]
1JJ2X-ray2.40M2-187[»]
1K73X-ray3.01O2-187[»]
1K8AX-ray3.00O2-187[»]
1K9MX-ray3.00O2-187[»]
1KC8X-ray3.01O2-187[»]
1KD1X-ray3.00O2-187[»]
1KQSX-ray3.10M2-187[»]
1M1KX-ray3.20O2-187[»]
1M90X-ray2.80O2-187[»]
1N8RX-ray3.00O2-187[»]
1NJIX-ray3.00O2-187[»]
1Q7YX-ray3.20O2-187[»]
1Q81X-ray2.95O2-187[»]
1Q82X-ray2.98O2-187[»]
1Q86X-ray3.00O2-187[»]
1QVFX-ray3.10M2-187[»]
1QVGX-ray2.90M2-187[»]
1S72X-ray2.40N1-187[»]
1VQ4X-ray2.70N1-187[»]
1VQ5X-ray2.60N1-187[»]
1VQ6X-ray2.70N1-187[»]
1VQ7X-ray2.50N1-187[»]
1VQ8X-ray2.20N1-187[»]
1VQ9X-ray2.40N1-187[»]
1VQKX-ray2.30N1-187[»]
1VQLX-ray2.30N1-187[»]
1VQMX-ray2.30N1-187[»]
1VQNX-ray2.40N1-187[»]
1VQOX-ray2.20N1-187[»]
1VQPX-ray2.25N1-187[»]
1W2BX-ray3.50M2-186[»]
1YHQX-ray2.40N1-187[»]
1YI2X-ray2.65N1-187[»]
1YIJX-ray2.60N1-187[»]
1YITX-ray2.80N1-187[»]
1YJ9X-ray2.90N1-187[»]
1YJNX-ray3.00N1-187[»]
1YJWX-ray2.90N1-187[»]
2B9NX-ray6.76S2-187[»]
2B9PX-ray6.46S2-187[»]
2OTJX-ray2.90N1-187[»]
2OTLX-ray2.70N1-187[»]
2QA4X-ray3.00N1-187[»]
2QEXX-ray2.90N1-187[»]
3CC2X-ray2.40N1-187[»]
3CC4X-ray2.70N1-187[»]
3CC7X-ray2.70N1-187[»]
3CCEX-ray2.75N1-187[»]
3CCJX-ray2.70N1-187[»]
3CCLX-ray2.90N1-187[»]
3CCMX-ray2.55N1-187[»]
3CCQX-ray2.90N1-187[»]
3CCRX-ray3.00N1-187[»]
3CCSX-ray2.95N1-187[»]
3CCUX-ray2.80N1-187[»]
3CCVX-ray2.90N1-187[»]
3CD6X-ray2.75N1-187[»]
3CMAX-ray2.80N1-187[»]
3CMEX-ray2.95N1-187[»]
3CPWX-ray2.70M1-187[»]
3CXCX-ray3.00M2-186[»]
3G4SX-ray3.20N2-187[»]
3G6EX-ray2.70N2-187[»]
3G71X-ray2.85N2-187[»]
3I55X-ray3.11N1-187[»]
3I56X-ray2.90N1-187[»]
3OW2X-ray2.70M2-187[»]
4HUBX-ray2.40N1-187[»]
ProteinModelPortalP14123.
SMRP14123. Positions 2-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46511; AAV46511; rrnAC1593.
GeneID3127918.
KEGGhma:rrnAC1593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0256.
HOGENOMHOG000105947.
KOK02881.
OMAEYGWEAP.
ProtClustDBPRK08569.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1449-MONOMER.

Family and domain databases

HAMAPMF_01337_A. Ribosomal_L18_A.
InterProIPR005485. Rbsml_L5_euk/L18_arc.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERPTHR23410. PTHR23410. 1 hit.
PfamPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSPR00058. RIBOSOMALL5.
ProtoNetSearch...

Other

EvolutionaryTraceP14123.

Entry information

Entry nameRL18_HALMA
AccessionPrimary (citable) accession number: P14123
Secondary accession number(s): Q5V1U1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 113 of the entry and version 3 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