Skip Header

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

P12732

- RL23_HALMA

UniProt

P12732 - RL23_HALMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

50S ribosomal protein L23P

Gene

rpl23p

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Binds to a specific region on the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. rRNA binding Source: UniProtKB-HAMAP
  3. 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-1465-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L23PUniRule annotation
Alternative name(s):
Hl25
Hmal23
L21
Gene namesi
Name:rpl23pUniRule annotation
Ordered Locus Names:rrnAC1609
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 – 11Removed2 Publications
Chaini2 – 858450S ribosomal protein L23PPRO_0000129435Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts with protein L29 and weakly with protein L39e.2 PublicationsUniRule annotation

Protein-protein interaction databases

STRINGi272569.rrnAC1609.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Helixi13 – 219
Beta strandi24 – 296
Helixi35 – 4612
Beta strandi50 – 578
Beta strandi61 – 699
Beta strandi71 – 733
Helixi75 – 795

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40P2-85[»]
1JJ2X-ray2.40R2-85[»]
1K73X-ray3.01T2-85[»]
1K8AX-ray3.00T2-85[»]
1K9MX-ray3.00T2-85[»]
1KC8X-ray3.01T2-85[»]
1KD1X-ray3.00T2-85[»]
1KQSX-ray3.10R2-85[»]
1M1KX-ray3.20T2-85[»]
1M90X-ray2.80T2-85[»]
1N8RX-ray3.00T2-85[»]
1NJIX-ray3.00T2-85[»]
1Q7YX-ray3.20T2-85[»]
1Q81X-ray2.95T2-85[»]
1Q82X-ray2.98T2-85[»]
1Q86X-ray3.00T2-85[»]
1QVFX-ray3.10R2-85[»]
1QVGX-ray2.90R2-85[»]
1S72X-ray2.40S1-85[»]
1VQ4X-ray2.70S1-85[»]
1VQ5X-ray2.60S1-85[»]
1VQ6X-ray2.70S1-85[»]
1VQ7X-ray2.50S1-85[»]
1VQ8X-ray2.20S1-85[»]
1VQ9X-ray2.40S1-85[»]
1VQKX-ray2.30S1-85[»]
1VQLX-ray2.30S1-85[»]
1VQMX-ray2.30S1-85[»]
1VQNX-ray2.40S1-85[»]
1VQOX-ray2.20S1-85[»]
1VQPX-ray2.25S1-85[»]
1W2BX-ray3.50R2-85[»]
1YHQX-ray2.40S1-85[»]
1YI2X-ray2.65S1-85[»]
1YIJX-ray2.60S1-85[»]
1YITX-ray2.80S1-85[»]
1YJ9X-ray2.90S1-85[»]
1YJNX-ray3.00S1-85[»]
1YJWX-ray2.90S1-85[»]
2B9NX-ray6.76X2-85[»]
2B9PX-ray6.46X2-85[»]
2OTJX-ray2.90S1-85[»]
2OTLX-ray2.70S1-85[»]
2QA4X-ray3.00S1-85[»]
2QEXX-ray2.90S1-85[»]
3CC2X-ray2.40S1-85[»]
3CC4X-ray2.70S1-85[»]
3CC7X-ray2.70S1-85[»]
3CCEX-ray2.75S1-85[»]
3CCJX-ray2.70S1-85[»]
3CCLX-ray2.90S1-85[»]
3CCMX-ray2.55S1-85[»]
3CCQX-ray2.90S1-85[»]
3CCRX-ray3.00S1-85[»]
3CCSX-ray2.95S1-85[»]
3CCUX-ray2.80S1-85[»]
3CCVX-ray2.90S1-85[»]
3CD6X-ray2.75S1-85[»]
3CMAX-ray2.80S1-85[»]
3CMEX-ray2.95S1-85[»]
3CPWX-ray2.70R1-85[»]
3CXCX-ray3.00R2-85[»]
3G4SX-ray3.20S2-82[»]
3G6EX-ray2.70S2-82[»]
3G71X-ray2.85S2-82[»]
3I55X-ray3.11S1-85[»]
3I56X-ray2.90S1-85[»]
3OW2X-ray2.70R2-82[»]
4ADXelectron microscopy6.60S1-85[»]
4HUBX-ray2.40S1-85[»]
ProteinModelPortaliP12732.
SMRiP12732. Positions 2-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12732.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L23P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0089.
HOGENOMiHOG000231364.
KOiK02892.
OMAiQNTLTFI.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_01369_A. Ribosomal_L23_A.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR019985. Ribosomal_L23.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
PfamiPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
TIGRFAMsiTIGR03636. L23_arch. 1 hit.
PROSITEiPS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12732-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSWDVIKHPH VTEKAMNDMD FQNKLQFAVD DRASKGEVAD AVEEQYDVTV
60 70 80
EQVNTQNTMD GEKKAVVRLS EDDDAQEVAS RIGVF
Length:85
Mass (Da):9,602
Last modified:January 23, 2007 - v2
Checksum:i2A2E869D640D5B60
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05222 Genomic DNA. Translation: AAA86861.1.
AY596297 Genomic DNA. Translation: AAV46526.1.
PIRiE35063. R5HS23.
RefSeqiYP_136232.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46526; AAV46526; rrnAC1609.
GeneIDi3128415.
KEGGihma:rrnAC1609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05222 Genomic DNA. Translation: AAA86861.1 .
AY596297 Genomic DNA. Translation: AAV46526.1 .
PIRi E35063. R5HS23.
RefSeqi YP_136232.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FFK X-ray 2.40 P 2-85 [» ]
1JJ2 X-ray 2.40 R 2-85 [» ]
1K73 X-ray 3.01 T 2-85 [» ]
1K8A X-ray 3.00 T 2-85 [» ]
1K9M X-ray 3.00 T 2-85 [» ]
1KC8 X-ray 3.01 T 2-85 [» ]
1KD1 X-ray 3.00 T 2-85 [» ]
1KQS X-ray 3.10 R 2-85 [» ]
1M1K X-ray 3.20 T 2-85 [» ]
1M90 X-ray 2.80 T 2-85 [» ]
1N8R X-ray 3.00 T 2-85 [» ]
1NJI X-ray 3.00 T 2-85 [» ]
1Q7Y X-ray 3.20 T 2-85 [» ]
1Q81 X-ray 2.95 T 2-85 [» ]
1Q82 X-ray 2.98 T 2-85 [» ]
1Q86 X-ray 3.00 T 2-85 [» ]
1QVF X-ray 3.10 R 2-85 [» ]
1QVG X-ray 2.90 R 2-85 [» ]
1S72 X-ray 2.40 S 1-85 [» ]
1VQ4 X-ray 2.70 S 1-85 [» ]
1VQ5 X-ray 2.60 S 1-85 [» ]
1VQ6 X-ray 2.70 S 1-85 [» ]
1VQ7 X-ray 2.50 S 1-85 [» ]
1VQ8 X-ray 2.20 S 1-85 [» ]
1VQ9 X-ray 2.40 S 1-85 [» ]
1VQK X-ray 2.30 S 1-85 [» ]
1VQL X-ray 2.30 S 1-85 [» ]
1VQM X-ray 2.30 S 1-85 [» ]
1VQN X-ray 2.40 S 1-85 [» ]
1VQO X-ray 2.20 S 1-85 [» ]
1VQP X-ray 2.25 S 1-85 [» ]
1W2B X-ray 3.50 R 2-85 [» ]
1YHQ X-ray 2.40 S 1-85 [» ]
1YI2 X-ray 2.65 S 1-85 [» ]
1YIJ X-ray 2.60 S 1-85 [» ]
1YIT X-ray 2.80 S 1-85 [» ]
1YJ9 X-ray 2.90 S 1-85 [» ]
1YJN X-ray 3.00 S 1-85 [» ]
1YJW X-ray 2.90 S 1-85 [» ]
2B9N X-ray 6.76 X 2-85 [» ]
2B9P X-ray 6.46 X 2-85 [» ]
2OTJ X-ray 2.90 S 1-85 [» ]
2OTL X-ray 2.70 S 1-85 [» ]
2QA4 X-ray 3.00 S 1-85 [» ]
2QEX X-ray 2.90 S 1-85 [» ]
3CC2 X-ray 2.40 S 1-85 [» ]
3CC4 X-ray 2.70 S 1-85 [» ]
3CC7 X-ray 2.70 S 1-85 [» ]
3CCE X-ray 2.75 S 1-85 [» ]
3CCJ X-ray 2.70 S 1-85 [» ]
3CCL X-ray 2.90 S 1-85 [» ]
3CCM X-ray 2.55 S 1-85 [» ]
3CCQ X-ray 2.90 S 1-85 [» ]
3CCR X-ray 3.00 S 1-85 [» ]
3CCS X-ray 2.95 S 1-85 [» ]
3CCU X-ray 2.80 S 1-85 [» ]
3CCV X-ray 2.90 S 1-85 [» ]
3CD6 X-ray 2.75 S 1-85 [» ]
3CMA X-ray 2.80 S 1-85 [» ]
3CME X-ray 2.95 S 1-85 [» ]
3CPW X-ray 2.70 R 1-85 [» ]
3CXC X-ray 3.00 R 2-85 [» ]
3G4S X-ray 3.20 S 2-82 [» ]
3G6E X-ray 2.70 S 2-82 [» ]
3G71 X-ray 2.85 S 2-82 [» ]
3I55 X-ray 3.11 S 1-85 [» ]
3I56 X-ray 2.90 S 1-85 [» ]
3OW2 X-ray 2.70 R 2-82 [» ]
4ADX electron microscopy 6.60 S 1-85 [» ]
4HUB X-ray 2.40 S 1-85 [» ]
ProteinModelPortali P12732.
SMRi P12732. Positions 2-85.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC1609.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV46526 ; AAV46526 ; rrnAC1609 .
GeneIDi 3128415.
KEGGi hma:rrnAC1609.

Phylogenomic databases

eggNOGi COG0089.
HOGENOMi HOG000231364.
KOi K02892.
OMAi QNTLTFI.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-1465-MONOMER.

Miscellaneous databases

EvolutionaryTracei P12732.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
HAMAPi MF_01369_A. Ribosomal_L23_A.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR019985. Ribosomal_L23.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view ]
Pfami PF00276. Ribosomal_L23. 1 hit.
[Graphical view ]
SUPFAMi SSF54189. SSF54189. 1 hit.
TIGRFAMsi TIGR03636. L23_arch. 1 hit.
PROSITEi PS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui."
    Hatakeyama T., Kimura M.
    Eur. J. Biochem. 172:703-711(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-85.
  2. "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].
  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 2-23.
  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 nameiRL23_HALMA
AccessioniPrimary (citable) accession number: P12732
Secondary accession number(s): Q5V1S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 117 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