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Reviewed, UniProtKB/Swiss-Prot P14135 (RL6_HALMA)

Last modified November 3, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L6P
Alternative name(s):
    Hmal6
    Hl10
Gene names
Name: rpl6p
Ordered Locus Names: rrnAC1596
OrganismHaloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier2238 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. HAMAP MF_01365

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with protein L13. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the ribosomal protein L6P family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 17817750S ribosomal protein L6P HAMAP MF_01365
PRO_0000131083

Natural variations

Natural variant31R → S
Natural variant241E → S

Secondary structure

.................................... 178
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14135-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 380872452165689C

FASTA17819,944
        10         20         30         40         50         60 
MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPDID VSVDGDTVVI ESDEDNAKTM 

        70         80         90        100        110        120 
STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG DEVVIENFLG EKAPRRTTIH 

       130        140        150        160        170 
GDTDVEIDGE ELTVSGPDIE AVGQTAADIE QLTRINDKDV RVFQDGVYIT RKPNRGDA 

« 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: 1832208] [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: 15520287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[3]"The N-terminal sequence of ribosomal protein L10 from the archaebacterium Halobacterium marismortui and its relationship to eubacterial protein L6 and other ribosomal proteins."
Dijk J., van den Broek R., Nasiulas G., Beck A., Reinhardt R., Wittmann-Liebold B.
Biol. Chem. Hoppe-Seyler 368:921-925(1987) [PubMed: 3311072] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-55.
[4]"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: 3196689] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
[5]"Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit."
Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.
Nature 400:841-847(1999) [PubMed: 10476961] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[6]"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: 10937989] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[7]"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: 10937990] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[8]"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: 11828326] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[9]"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: 11483524] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[10]"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: 12150912] [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.
[11]"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: 12185246] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[12]"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: 12860128] [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.
[13]"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: 14561884] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

X58395 Genomic DNA. Translation: CAA41287.1.
AY596297 Genomic DNA. Translation: AAV46514.1.
PIRR5HS6L. S16538.
RefSeqYP_136220.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1C04X-ray5.00B22-158[»]
1FFKX-ray2.4012-178[»]
1JJ2X-ray2.40E2-178[»]
1K73X-ray3.01G2-178[»]
1K8AX-ray3.00G2-178[»]
1K9MX-ray3.00G2-178[»]
1KC8X-ray3.01G2-178[»]
1KD1X-ray3.00G2-178[»]
1KQSX-ray3.10E2-178[»]
1M1KX-ray3.20G2-178[»]
1M90X-ray2.80G2-178[»]
1N8RX-ray3.00G2-178[»]
1NJIX-ray3.00G2-178[»]
1Q7YX-ray3.20G2-178[»]
1Q81X-ray2.95G2-178[»]
1Q82X-ray2.98G2-178[»]
1Q86X-ray3.00G2-178[»]
1QVFX-ray3.10E2-178[»]
1QVGX-ray2.90E2-178[»]
1S72X-ray2.40E1-178[»]
1VQ4X-ray2.70E1-178[»]
1VQ5X-ray2.60E1-178[»]
1VQ6X-ray2.70E1-178[»]
1VQ7X-ray2.50E1-178[»]
1VQ8X-ray2.20E1-178[»]
1VQ9X-ray2.40E1-178[»]
1VQKX-ray2.30E1-178[»]
1VQLX-ray2.30E1-178[»]
1VQMX-ray2.30E1-178[»]
1VQNX-ray2.40E1-178[»]
1VQOX-ray2.20E1-178[»]
1VQPX-ray2.25E1-178[»]
1W2BX-ray3.50E2-177[»]
1YHQX-ray2.40E1-178[»]
1YI2X-ray2.65E1-178[»]
1YIJX-ray2.60E1-178[»]
1YITX-ray2.80E1-178[»]
1YJ9X-ray2.90E1-178[»]
1YJNX-ray3.00E1-178[»]
1YJWX-ray2.90E1-178[»]
2OTJX-ray2.90E1-178[»]
2OTLX-ray2.70E1-178[»]
2QA4X-ray3.00E1-178[»]
2QEXX-ray2.90E1-178[»]
3CC2X-ray2.40E1-178[»]
3CC4X-ray2.70E1-178[»]
3CC7X-ray2.70E1-178[»]
3CCEX-ray2.75E1-178[»]
3CCJX-ray2.70E1-178[»]
3CCLX-ray2.90E1-178[»]
3CCMX-ray2.55E1-178[»]
3CCQX-ray2.90E1-178[»]
3CCRX-ray3.00E1-178[»]
3CCSX-ray2.95E1-178[»]
3CCUX-ray2.80E1-178[»]
3CCVX-ray2.90E1-178[»]
3CD6X-ray2.75E1-178[»]
3CMAX-ray2.80E1-178[»]
3CMEX-ray2.95E1-178[»]
3CPWX-ray2.70E1-178[»]
3CXCX-ray3.00E2-178[»]
3G4SX-ray3.20E2-173[»]
3G6EX-ray2.70E2-173[»]
3G71X-ray2.85E2-173[»]
ModBaseSearch...

Genome annotation databases

GeneID3127517.
GenomeReviewsGene locus rrnAC1596 in contig AY596297_GR.
KEGGhma:rrnAC1596.
NMPDRfig|272569.1.peg.1487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP14135.
OMAQLTRIND.

Enzyme and pathway databases

BioCycHMAR272569:RRNAC1596-MON.

Family and domain databases

HAMAPMF_01365.
[Tree]
InterProIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
IPR019907. Ribosomal_L6P_arc.
[Graphical view]
Gene3DG3DSA:3.90.930.12. Ribosomal_L6. 2 hits.
PANTHERPTHR11655. Ribosomal_L6. 1 hit.
PfamPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFPIRSF002162. Ribosomal_L6. 1 hit.
TIGRFAMsTIGR03653. Arch_L6P. 1 hit.
PROSITEPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRL6_HALMA
AccessionPrimary (citable) accession number: P14135
Secondary accession number(s): P12739, Q5V1T8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents