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Protein

50S ribosomal protein L30P

Gene

rpl30p

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, stabilizing the orientation of adjacent RNA domains.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  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-1447-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L30PUniRule annotation
Alternative name(s):
Hl16
Hl20
Hmal30
Gene namesi
Name:rpl30pUniRule annotation
Ordered Locus Names:rrnAC1591
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. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15415450S ribosomal protein L30PPRO_0000104622Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Binds 5S rRNA.2 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi272569.rrnAC1591.

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi15 – 239Combined sources
Beta strandi31 – 355Combined sources
Helixi39 – 479Combined sources
Helixi49 – 513Combined sources
Beta strandi52 – 554Combined sources
Helixi59 – 6911Combined sources
Beta strandi72 – 754Combined sources
Helixi81 – 877Combined sources
Beta strandi88 – 925Combined sources
Helixi93 – 1019Combined sources
Helixi108 – 1103Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi128 – 1314Combined sources
Helixi132 – 1343Combined sources
Beta strandi137 – 1404Combined sources
Helixi143 – 15210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40T1-154[»]
1JJ2X-ray2.40V1-154[»]
1K73X-ray3.01X1-154[»]
1K8AX-ray3.00X1-154[»]
1K9MX-ray3.00X1-154[»]
1KC8X-ray3.01X1-154[»]
1KD1X-ray3.00X1-154[»]
1KQSX-ray3.10V1-154[»]
1M1KX-ray3.20X1-154[»]
1M90X-ray2.80X1-154[»]
1N8RX-ray3.00X1-154[»]
1NJIX-ray3.00X1-154[»]
1Q7YX-ray3.20X1-154[»]
1Q81X-ray2.95X1-154[»]
1Q82X-ray2.98X1-154[»]
1Q86X-ray3.00X1-154[»]
1QVFX-ray3.10V1-154[»]
1QVGX-ray2.90V1-154[»]
1S72X-ray2.40W1-154[»]
1VQ4X-ray2.70W1-154[»]
1VQ5X-ray2.60W1-154[»]
1VQ6X-ray2.70W1-154[»]
1VQ7X-ray2.50W1-154[»]
1VQ8X-ray2.20W1-154[»]
1VQ9X-ray2.40W1-154[»]
1VQKX-ray2.30W1-154[»]
1VQLX-ray2.30W1-154[»]
1VQMX-ray2.30W1-154[»]
1VQNX-ray2.40W1-154[»]
1VQOX-ray2.20W1-154[»]
1VQPX-ray2.25W1-154[»]
1W2BX-ray3.50V1-154[»]
1YHQX-ray2.40W1-154[»]
1YI2X-ray2.65W1-154[»]
1YIJX-ray2.60W1-154[»]
1YITX-ray2.80W1-154[»]
1YJ9X-ray2.90W1-154[»]
1YJNX-ray3.00W1-154[»]
1YJWX-ray2.90W1-154[»]
2OTJX-ray2.90W1-154[»]
2OTLX-ray2.70W1-154[»]
2QA4X-ray3.00W1-154[»]
2QEXX-ray2.90W1-154[»]
3CC2X-ray2.40W1-154[»]
3CC4X-ray2.70W1-154[»]
3CC7X-ray2.70W1-154[»]
3CCEX-ray2.75W1-154[»]
3CCJX-ray2.70W1-154[»]
3CCLX-ray2.90W1-154[»]
3CCMX-ray2.55W1-154[»]
3CCQX-ray2.90W1-154[»]
3CCRX-ray3.00W1-154[»]
3CCSX-ray2.95W1-154[»]
3CCUX-ray2.80W1-154[»]
3CCVX-ray2.90W1-154[»]
3CD6X-ray2.75W1-154[»]
3CMAX-ray2.80W1-154[»]
3CMEX-ray2.95W1-154[»]
3CPWX-ray2.70V1-154[»]
3CXCX-ray3.00V1-154[»]
3G4SX-ray3.20W1-154[»]
3G6EX-ray2.70W1-154[»]
3G71X-ray2.85W1-154[»]
3I55X-ray3.11W1-154[»]
3I56X-ray2.90W1-154[»]
3OW2X-ray2.70V1-154[»]
4ADXelectron microscopy6.60W1-154[»]
4V9FX-ray2.40W1-154[»]
ProteinModelPortaliP14121.
SMRiP14121. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14121.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L30P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000170918.
KOiK02907.
OMAiHPPRKGH.

Family and domain databases

Gene3Di1.10.15.30. 1 hit.
3.30.1390.20. 2 hits.
HAMAPiMF_01371_A. Ribosomal_L30_A.
InterProiIPR005997. Ribosomal_L30_arc.
IPR023106. Ribosomal_L30_central_dom_arc.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
SUPFAMiSSF55129. SSF55129. 1 hit.
TIGRFAMsiTIGR01309. L30P_arch. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14121-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND
60 70 80 90 100
FVAFGEPSQE TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL
110 120 130 140 150
LSEETTLREQ GLSPTLRLHP PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL

EAMR
Length:154
Mass (Da):17,042
Last modified:August 1, 1992 - v2
Checksum:iED673F036E974C14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831W → L AA sequence (PubMed:2591382)Curated
Sequence conflicti148 – 1481Missing AA sequence (PubMed:2591382)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41292.1.
AY596297 Genomic DNA. Translation: AAV46509.1.
PIRiS16543. R5HS30.
RefSeqiYP_136215.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46509; AAV46509; rrnAC1591.
GeneIDi3127531.
KEGGihma:rrnAC1591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58395 Genomic DNA. Translation: CAA41292.1.
AY596297 Genomic DNA. Translation: AAV46509.1.
PIRiS16543. R5HS30.
RefSeqiYP_136215.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40T1-154[»]
1JJ2X-ray2.40V1-154[»]
1K73X-ray3.01X1-154[»]
1K8AX-ray3.00X1-154[»]
1K9MX-ray3.00X1-154[»]
1KC8X-ray3.01X1-154[»]
1KD1X-ray3.00X1-154[»]
1KQSX-ray3.10V1-154[»]
1M1KX-ray3.20X1-154[»]
1M90X-ray2.80X1-154[»]
1N8RX-ray3.00X1-154[»]
1NJIX-ray3.00X1-154[»]
1Q7YX-ray3.20X1-154[»]
1Q81X-ray2.95X1-154[»]
1Q82X-ray2.98X1-154[»]
1Q86X-ray3.00X1-154[»]
1QVFX-ray3.10V1-154[»]
1QVGX-ray2.90V1-154[»]
1S72X-ray2.40W1-154[»]
1VQ4X-ray2.70W1-154[»]
1VQ5X-ray2.60W1-154[»]
1VQ6X-ray2.70W1-154[»]
1VQ7X-ray2.50W1-154[»]
1VQ8X-ray2.20W1-154[»]
1VQ9X-ray2.40W1-154[»]
1VQKX-ray2.30W1-154[»]
1VQLX-ray2.30W1-154[»]
1VQMX-ray2.30W1-154[»]
1VQNX-ray2.40W1-154[»]
1VQOX-ray2.20W1-154[»]
1VQPX-ray2.25W1-154[»]
1W2BX-ray3.50V1-154[»]
1YHQX-ray2.40W1-154[»]
1YI2X-ray2.65W1-154[»]
1YIJX-ray2.60W1-154[»]
1YITX-ray2.80W1-154[»]
1YJ9X-ray2.90W1-154[»]
1YJNX-ray3.00W1-154[»]
1YJWX-ray2.90W1-154[»]
2OTJX-ray2.90W1-154[»]
2OTLX-ray2.70W1-154[»]
2QA4X-ray3.00W1-154[»]
2QEXX-ray2.90W1-154[»]
3CC2X-ray2.40W1-154[»]
3CC4X-ray2.70W1-154[»]
3CC7X-ray2.70W1-154[»]
3CCEX-ray2.75W1-154[»]
3CCJX-ray2.70W1-154[»]
3CCLX-ray2.90W1-154[»]
3CCMX-ray2.55W1-154[»]
3CCQX-ray2.90W1-154[»]
3CCRX-ray3.00W1-154[»]
3CCSX-ray2.95W1-154[»]
3CCUX-ray2.80W1-154[»]
3CCVX-ray2.90W1-154[»]
3CD6X-ray2.75W1-154[»]
3CMAX-ray2.80W1-154[»]
3CMEX-ray2.95W1-154[»]
3CPWX-ray2.70V1-154[»]
3CXCX-ray3.00V1-154[»]
3G4SX-ray3.20W1-154[»]
3G6EX-ray2.70W1-154[»]
3G71X-ray2.85W1-154[»]
3I55X-ray3.11W1-154[»]
3I56X-ray2.90W1-154[»]
3OW2X-ray2.70V1-154[»]
4ADXelectron microscopy6.60W1-154[»]
4V9FX-ray2.40W1-154[»]
ProteinModelPortaliP14121.
SMRiP14121. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46509; AAV46509; rrnAC1591.
GeneIDi3127531.
KEGGihma:rrnAC1591.

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000170918.
KOiK02907.
OMAiHPPRKGH.

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1447-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14121.

Family and domain databases

Gene3Di1.10.15.30. 1 hit.
3.30.1390.20. 2 hits.
HAMAPiMF_01371_A. Ribosomal_L30_A.
InterProiIPR005997. Ribosomal_L30_arc.
IPR023106. Ribosomal_L30_central_dom_arc.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
SUPFAMiSSF55129. SSF55129. 1 hit.
TIGRFAMsiTIGR01309. L30P_arch. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins."
    Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.
    Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  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 1-30.
  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 nameiRL30_HALMA
AccessioniPrimary (citable) accession number: P14121
Secondary accession number(s): Q5V1U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1992
Last modified: February 4, 2015
This is version 115 of the entry and version 2 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.