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Protein

50S ribosomal protein L24

Gene

rplX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.3 Publications
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.2 Publications

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • ribosomal large subunit assembly Source: CAFA
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10884-MONOMER
MetaCyc:EG10884-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L24
Alternative name(s):
Large ribosomal subunit protein uL241 Publication
Gene namesi
Name:rplX
Ordered Locus Names:b3309, JW3271
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10884 rplX

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: CAFA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001306542 – 10450S ribosomal protein L24Add BLAST103

Proteomic databases

EPDiP60624
PaxDbiP60624
PRIDEiP60624

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (PubMed:391595, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Might contact the SecYEG translocation complex when it is docked with the ribosome.1 Publication9 Publications

Protein-protein interaction databases

DIPiDIP-47846N
IntActiP60624 61 interactors.
STRINGi316385.ECDH10B_3484

Structurei

Secondary structure

1104
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Turni17 – 20Combined sources4
Beta strandi22 – 28Combined sources7
Beta strandi32 – 36Combined sources5
Beta strandi40 – 45Combined sources6
Helixi51 – 53Combined sources3
Beta strandi57 – 62Combined sources6
Helixi67 – 69Combined sources3
Beta strandi70 – 74Combined sources5
Turni75 – 78Combined sources4
Beta strandi79 – 81Combined sources3
Beta strandi83 – 88Combined sources6
Beta strandi91 – 96Combined sources6
Turni97 – 100Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00u2-104[»]
2J28electron microscopy8.00U2-103[»]
2RDOelectron microscopy9.10U2-104[»]
2VRHelectron microscopy19.00C2-104[»]
3BBXelectron microscopy10.00U2-104[»]
3J45electron microscopy9.50U2-104[»]
3J46electron microscopy10.10U2-104[»]
3J5Lelectron microscopy6.60U2-103[»]
3J7Zelectron microscopy3.90U1-104[»]
3J8Gelectron microscopy5.00U1-104[»]
3J9Yelectron microscopy3.90U1-104[»]
3J9Zelectron microscopy3.60LS2-104[»]
3JA1electron microscopy3.60LW2-104[»]
3JBUelectron microscopy3.64u1-104[»]
3JBVelectron microscopy3.32u1-104[»]
3JCDelectron microscopy3.70U1-104[»]
3JCEelectron microscopy3.20U1-104[»]
3JCJelectron microscopy3.70T1-104[»]
3JCNelectron microscopy4.60U1-104[»]
4CSUelectron microscopy5.50U2-104[»]
4U1UX-ray2.95BU/DU2-103[»]
4U1VX-ray3.00BU/DU2-103[»]
4U20X-ray2.90BU/DU2-103[»]
4U24X-ray2.90BU/DU2-103[»]
4U25X-ray2.90BU/DU2-103[»]
4U26X-ray2.80BU/DU2-103[»]
4U27X-ray2.80BU/DU2-103[»]
4UY8electron microscopy3.80U2-103[»]
4V47electron microscopy12.30AS2-104[»]
4V48electron microscopy11.50AS2-104[»]
4V4HX-ray3.46BU/DU1-104[»]
4V4QX-ray3.46BU/DU2-104[»]
4V4Velectron microscopy15.00BS4-102[»]
4V4Welectron microscopy15.00BS4-102[»]
4V50X-ray3.22BU/DU2-104[»]
4V52X-ray3.21BU/DU2-104[»]
4V53X-ray3.54BU/DU2-104[»]
4V54X-ray3.30BU/DU2-104[»]
4V55X-ray4.00BU/DU2-104[»]
4V56X-ray3.93BU/DU2-104[»]
4V57X-ray3.50BU/DU2-104[»]
4V5BX-ray3.74AU/CU2-104[»]
4V5Helectron microscopy5.80BU2-103[»]
4V5YX-ray4.45BU/DU2-104[»]
4V64X-ray3.50BU/DU2-104[»]
4V65electron microscopy9.00BO1-103[»]
4V66electron microscopy9.00BO1-103[»]
4V69electron microscopy6.70BU2-103[»]
4V6CX-ray3.19BU/DU1-104[»]
4V6DX-ray3.81BU/DU1-104[»]
4V6EX-ray3.71BU/DU1-104[»]
4V6Kelectron microscopy8.25AV1-104[»]
4V6Lelectron microscopy13.20BV1-104[»]
4V6Melectron microscopy7.10BU2-104[»]
4V6Nelectron microscopy12.10AW2-104[»]
4V6Oelectron microscopy14.70BW2-104[»]
4V6Pelectron microscopy13.50BW2-104[»]
4V6Qelectron microscopy11.50BW2-104[»]
4V6Relectron microscopy11.50BW2-104[»]
4V6Selectron microscopy13.10AW2-104[»]
4V6Telectron microscopy8.30BU2-103[»]
4V6Velectron microscopy9.80BY2-104[»]
4V6Yelectron microscopy12.00BU1-103[»]
4V6Zelectron microscopy12.00BU1-103[»]
4V70electron microscopy17.00BU1-103[»]
4V71electron microscopy20.00BU1-103[»]
4V72electron microscopy13.00BU1-103[»]
4V73electron microscopy15.00BU1-103[»]
4V74electron microscopy17.00BU1-103[»]
4V75electron microscopy12.00BU1-103[»]
4V76electron microscopy17.00BU1-103[»]
4V77electron microscopy17.00BU1-103[»]
4V78electron microscopy20.00BU1-103[»]
4V79electron microscopy15.00BU1-103[»]
4V7Aelectron microscopy9.00BU1-103[»]
4V7Belectron microscopy6.80BU1-104[»]
4V7Celectron microscopy7.60BW2-104[»]
4V7Delectron microscopy7.60AX2-104[»]
4V7Ielectron microscopy9.60AU1-104[»]
4V7SX-ray3.25BU/DU2-103[»]
4V7TX-ray3.19BU/DU2-103[»]
4V7UX-ray3.10BU/DU2-103[»]
4V7VX-ray3.29BU/DU2-103[»]
4V85X-ray3.20Y1-104[»]
4V89X-ray3.70BY1-104[»]
4V9CX-ray3.30BU/DU1-104[»]
4V9DX-ray3.00CU/DU2-103[»]
4V9OX-ray2.90AU/CU/EU/GU1-104[»]
4V9PX-ray2.90AU/CU/EU/GU1-104[»]
4WF1X-ray3.09BU/DU2-103[»]
4WOIX-ray3.00BU/CU1-104[»]
4WWWX-ray3.10RU/YU2-103[»]
4YBBX-ray2.10CV/DV2-103[»]
5ADYelectron microscopy4.50U1-104[»]
5AFIelectron microscopy2.90U1-104[»]
5AKAelectron microscopy5.70U2-104[»]
5GADelectron microscopy3.70V1-104[»]
5GAEelectron microscopy3.33V1-104[»]
5GAFelectron microscopy4.30V2-103[»]
5GAGelectron microscopy3.80V1-104[»]
5GAHelectron microscopy3.80V1-104[»]
5H5Uelectron microscopy3.00V2-104[»]
5IQRelectron microscopy3.00U1-104[»]
5IT8X-ray3.12CV/DV2-103[»]
5J5BX-ray2.80CV/DV2-103[»]
5J7LX-ray3.00CV/DV2-103[»]
5J88X-ray3.32CV/DV2-104[»]
5J8AX-ray3.10CV/DV2-104[»]
5J91X-ray2.96CV/DV2-104[»]
5JC9X-ray3.03CV/DV2-103[»]
5JTEelectron microscopy3.60BU1-104[»]
5JU8electron microscopy3.60BU1-104[»]
5KCRelectron microscopy3.601Y1-104[»]
5KCSelectron microscopy3.901Y1-104[»]
5KPSelectron microscopy3.90U1-104[»]
5KPVelectron microscopy4.10T1-104[»]
5KPWelectron microscopy3.90T1-104[»]
5KPXelectron microscopy3.90T1-104[»]
5L3Pelectron microscopy3.70Y1-104[»]
5LZAelectron microscopy3.60U2-103[»]
5LZBelectron microscopy5.30U2-103[»]
5LZCelectron microscopy4.80U2-103[»]
5LZDelectron microscopy3.40U2-103[»]
5LZEelectron microscopy3.50U2-103[»]
5LZFelectron microscopy4.60U2-103[»]
5MDVelectron microscopy2.97U1-104[»]
5MDWelectron microscopy3.06U1-104[»]
5MDYelectron microscopy3.35U1-104[»]
5MDZelectron microscopy3.10U1-104[»]
5MGPelectron microscopy3.10U2-103[»]
5NCOelectron microscopy4.80V2-103[»]
5NP6electron microscopy3.60s2-103[»]
5NWYelectron microscopy2.93h1-104[»]
5O2Relectron microscopy3.40U2-103[»]
5U4Ielectron microscopy3.50V1-104[»]
5U9Felectron microscopy3.20231-104[»]
5U9Gelectron microscopy3.20231-104[»]
5UYKelectron microscopy3.90232-103[»]
5UYLelectron microscopy3.60232-103[»]
5UYMelectron microscopy3.20232-103[»]
5UYNelectron microscopy4.00232-103[»]
5UYPelectron microscopy3.90232-103[»]
5UYQelectron microscopy3.80232-103[»]
6BU8electron microscopy3.50232-103[»]
6C4Ielectron microscopy3.24V1-104[»]
6ENFelectron microscopy3.20U2-103[»]
6ENJelectron microscopy3.70U2-103[»]
6ENUelectron microscopy3.10U2-103[»]
ProteinModelPortaliP60624
SMRiP60624
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60624

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105KAR Bacteria
COG0198 LUCA
HOGENOMiHOG000039892
InParanoidiP60624
KOiK02895
OMAiPQGGIVE
PhylomeDBiP60624

Family and domain databases

Gene3Di2.30.30.301 hit
HAMAPiMF_01326_B Ribosomal_L24_B, 1 hit
InterProiView protein in InterPro
IPR005824 KOW
IPR014722 Rib_L2_dom2
IPR003256 Ribosomal_L24
IPR005825 Ribosomal_L24/26_CS
IPR008991 Translation_prot_SH3-like_sf
PANTHERiPTHR12903 PTHR12903, 1 hit
PfamiView protein in Pfam
PF00467 KOW, 1 hit
PF17136 ribosomal_L24, 1 hit
SMARTiView protein in SMART
SM00739 KOW, 1 hit
SUPFAMiSSF50104 SSF50104, 1 hit
TIGRFAMsiTIGR01079 rplX_bact, 1 hit
PROSITEiView protein in PROSITE
PS01108 RIBOSOMAL_L24, 1 hit

Sequencei

Sequence statusi: Complete.

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

P60624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKIRRDDE VIVLTGKDKG KRGKVKNVLS SGKVIVEGIN LVKKHQKPVP
60 70 80 90 100
ALNQPGGIVE KEAAIQVSNV AIFNAATGKA DRVGFRFEDG KKVRFFKSNS

ETIK
Length:104
Mass (Da):11,316
Last modified:January 23, 2007 - v2
Checksum:i0ABF7DD305FA07F5
GO

Mass spectrometryi

Molecular mass is 11186.5 Da from positions 2 - 104. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25716.1
U18997 Genomic DNA Translation: AAA58106.1
U00096 Genomic DNA Translation: AAC76334.1
AP009048 Genomic DNA Translation: BAE77982.1
M10195 Genomic DNA Translation: AAA24050.1
PIRiH65123 R5EC24
RefSeqiNP_417768.1, NC_000913.3
WP_000729185.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76334; AAC76334; b3309
BAE77982; BAE77982; BAE77982
GeneIDi29456670
947810
KEGGiecj:JW3271
eco:b3309
PATRICifig|1411691.4.peg.3422

Similar proteinsi

Entry informationi

Entry nameiRL24_ECOLI
AccessioniPrimary (citable) accession number: P60624
Secondary accession number(s): P02425, P37438, Q2M6X4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 154 of the entry and version 2 of the sequence. See 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