Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L18

Gene

rpl18

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

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.

GO - Molecular functioni

  1. 5S rRNA binding Source: InterPro
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1449-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L18
Alternative name(s):
Hl12
Hmal18
Gene namesi
Name:rpl18
Ordered Locus Names:rrnAC1593
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18718650S ribosomal protein L18PRO_0000131400Add
BLAST

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1593.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi12 – 154Combined sources
Helixi21 – 288Combined sources
Beta strandi34 – 396Combined sources
Beta strandi44 – 507Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 648Combined sources
Helixi65 – 706Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 9517Combined sources
Beta strandi102 – 1043Combined sources
Helixi115 – 12511Combined sources
Helixi134 – 1363Combined sources
Helixi140 – 1445Combined sources
Helixi146 – 1538Combined sources
Beta strandi159 – 1624Combined sources
Helixi166 – 1683Combined sources
Helixi170 – 18112Combined sources
Beta strandi182 – 1854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40K2-186[»]
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-ray3.50M2-187[»]
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[»]
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-ray3.00M2-187[»]
3G4SX-ray3.20N2-187[»]
3G6EX-ray2.70N2-187[»]
3G71X-ray2.85N2-187[»]
3I55X-ray3.11N1-187[»]
3I56X-ray2.90N1-187[»]
3OW2X-ray2.70M2-187[»]
4ADXelectron microscopy6.60N1-187[»]
4V4RX-ray5.90S2-187[»]
4V4SX-ray6.76S2-187[»]
4V4TX-ray6.46S2-187[»]
4V9FX-ray2.40N1-187[»]
ProteinModelPortaliP14123.
SMRiP14123. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14123.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiCOG0256.
HOGENOMiHOG000105947.
KOiK02881.
OMAiEYGWEAP.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14123-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT
60 70 80 90 100
LGPNGDDTLA SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE
110 120 130 140 150
AVLDIGLNSP TPGSKVFAIQ EGAIDAGLDI PHNDDVLADW QRTRGAHIAE
160 170 180
YDEQLEEPLY SGDFDAADLP EHFDELRETL LDGDIEL
Length:187
Mass (Da):20,614
Last modified:January 23, 2007 - v3
Checksum:i60E9AF3CB64E7CA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181R → A AA sequence (PubMed:3196689)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.
PIRiS16541. R5HS18.
RefSeqiWP_011223738.1. NC_006396.1.
YP_136217.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46511; AAV46511; rrnAC1593.
GeneIDi3127918.
KEGGihma:rrnAC1593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.
PIRiS16541. R5HS18.
RefSeqiWP_011223738.1. NC_006396.1.
YP_136217.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40K2-186[»]
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-ray3.50M2-187[»]
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[»]
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-ray3.00M2-187[»]
3G4SX-ray3.20N2-187[»]
3G6EX-ray2.70N2-187[»]
3G71X-ray2.85N2-187[»]
3I55X-ray3.11N1-187[»]
3I56X-ray2.90N1-187[»]
3OW2X-ray2.70M2-187[»]
4ADXelectron microscopy6.60N1-187[»]
4V4RX-ray5.90S2-187[»]
4V4SX-ray6.76S2-187[»]
4V4TX-ray6.46S2-187[»]
4V9FX-ray2.40N1-187[»]
ProteinModelPortaliP14123.
SMRiP14123. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46511; AAV46511; rrnAC1593.
GeneIDi3127918.
KEGGihma:rrnAC1593.

Phylogenomic databases

eggNOGiCOG0256.
HOGENOMiHOG000105947.
KOiK02881.
OMAiEYGWEAP.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1449-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14123.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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 nameiRL18_HALMA
AccessioniPrimary (citable) accession number: P14123
Secondary accession number(s): Q5V1U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 120 of the entry and version 3 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.