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P10970 (RL22_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 109. 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 L22P
Alternative name(s):
Hl23
Hmal22
Gene names
Name:rpl22p
Ordered Locus Names:rrnAC1606
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 length155 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 specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome By similarity. HAMAP-Rule MF_01331

Contacts all 6 domains of the 23S rRNA, helping stabilize their relative orientation. An extended beta-hairpin in the C-terminus forms part of the polypeptide exit tunnel, in which it helps forms a bend with protein L4, while most of the rest of the protein is located at the polypeptide exit tunnel on the outside of the subunit. HAMAP-Rule MF_01331

Subunit structure

Part of the 50S ribosomal subunit. Contacts the macrolide antibiotic tylosin in the polypeptide exit tunnel. 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 L22P 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_componentlarge ribosomal subunit

Inferred from electronic annotation. Source: InterPro

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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.4
Chain2 – 15515450S ribosomal protein L22P HAMAP-Rule MF_01331
PRO_0000125272

Secondary structure

......................... 155
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10970 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E6730272296C0D7C

FASTA15516,941
        10         20         30         40         50         60 
MGISYSVEAD PDTTAKAMLR ERQMSFKHSK AIAREIKGKT AGEAVDYLEA VIEGDQPVPF 

        70         80         90        100        110        120 
KQHNSGVGHK SKVDGWDAGR YPEKASKAFL DLLENAVGNA DHQGFDGEAM TIKHVAAHKV 

       130        140        150 
GEQQGRKPRA MGRASAWNSP QVDVELILEE PEVED 

« Hide

References

« Hide 'large scale' references
[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]"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]"The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui."
Hatakeyama T., Hatakeyama T., Kimura M.
FEBS Lett. 240:21-28(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-155.
[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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-27.
[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
J05222 Genomic DNA. Translation: AAA86864.1.
AY596297 Genomic DNA. Translation: AAV46523.1.
PIRR5HS22. H35063.
RefSeqYP_136229.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40O2-155[»]
1JJ2X-ray2.40Q2-155[»]
1K73X-ray3.01S2-155[»]
1K8AX-ray3.00S2-155[»]
1K9MX-ray3.00S2-155[»]
1KC8X-ray3.01S2-155[»]
1KD1X-ray3.00S2-155[»]
1KQSX-ray3.10Q2-155[»]
1M1KX-ray3.20S2-155[»]
1M90X-ray2.80S2-155[»]
1N8RX-ray3.00S2-155[»]
1NJIX-ray3.00S2-155[»]
1Q7YX-ray3.20S2-155[»]
1Q81X-ray2.95S2-155[»]
1Q82X-ray2.98S2-155[»]
1Q86X-ray3.00S2-155[»]
1QVFX-ray3.10Q2-155[»]
1QVGX-ray2.90Q2-155[»]
1S72X-ray2.40R1-155[»]
1VQ4X-ray2.70R1-155[»]
1VQ5X-ray2.60R1-155[»]
1VQ6X-ray2.70R1-155[»]
1VQ7X-ray2.50R1-155[»]
1VQ8X-ray2.20R1-155[»]
1VQ9X-ray2.40R1-155[»]
1VQKX-ray2.30R1-155[»]
1VQLX-ray2.30R1-155[»]
1VQMX-ray2.30R1-155[»]
1VQNX-ray2.40R1-155[»]
1VQOX-ray2.20R1-155[»]
1VQPX-ray2.25R1-155[»]
1W2BX-ray3.50Q2-154[»]
1YHQX-ray2.40R1-155[»]
1YI2X-ray2.65R1-155[»]
1YIJX-ray2.60R1-155[»]
1YITX-ray2.80R1-155[»]
1YJ9X-ray2.90R1-155[»]
1YJNX-ray3.00R1-155[»]
1YJWX-ray2.90R1-155[»]
2OTJX-ray2.90R1-155[»]
2OTLX-ray2.70R1-155[»]
2QA4X-ray3.00R1-155[»]
2QEXX-ray2.90R1-155[»]
3CC2X-ray2.40R1-155[»]
3CC4X-ray2.70R1-155[»]
3CC7X-ray2.70R1-155[»]
3CCEX-ray2.75R1-155[»]
3CCJX-ray2.70R1-155[»]
3CCLX-ray2.90R1-155[»]
3CCMX-ray2.55R1-155[»]
3CCQX-ray2.90R1-155[»]
3CCRX-ray3.00R1-155[»]
3CCSX-ray2.95R1-155[»]
3CCUX-ray2.80R1-155[»]
3CCVX-ray2.90R1-155[»]
3CD6X-ray2.75R1-155[»]
3CMAX-ray2.80R1-155[»]
3CMEX-ray2.95R1-155[»]
3CPWX-ray2.70Q1-155[»]
3CXCX-ray3.00Q2-154[»]
3G4SX-ray3.20R2-151[»]
3G6EX-ray2.70R2-151[»]
3G71X-ray2.85R2-151[»]
3I55X-ray3.11R1-155[»]
3I56X-ray2.90R1-155[»]
3OW2X-ray2.70Q2-151[»]
4HUBX-ray2.40R1-155[»]
ProteinModelPortalP10970.
SMRP10970. Positions 2-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46523; AAV46523; rrnAC1606.
GeneID3128443.
KEGGhma:rrnAC1606.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0091.
HOGENOMHOG000205045.
KOK02890.
OMAMHIRKAN.
ProtClustDBPRK04223.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1462-MONOMER.

Family and domain databases

Gene3D3.90.470.10. 1 hit.
HAMAPMF_01331_A. Ribosomal_L22_A.
InterProIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERPTHR11593. PTHR11593. 1 hit.
PfamPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMSSF54843. SSF54843. 1 hit.
TIGRFAMsTIGR01038. L22_arch. 1 hit.
PROSITEPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10970.

Entry information

Entry nameRL22_HALMA
AccessionPrimary (citable) accession number: P10970
Secondary accession number(s): Q5V1S9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 109 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