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Protein

50S ribosomal protein L29

Gene

rpmC

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

Functioni

Binds 23S rRNA. It is not essential for growth.2 Publications
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).1 Publication

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10887-MONOMER
MetaCyc:EG10887-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L29
Alternative name(s):
Large ribosomal subunit protein uL291 Publication
Gene namesi
Name:rpmC
Ordered Locus Names:b3312, JW3274
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10887 rpmC

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Cells missing both S17 and L29 grow very slowly and have a rather unstable temperature-sensitive phenotype.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001303841 – 6350S ribosomal protein L29Add BLAST63

Proteomic databases

EPDiP0A7M6
PaxDbiP0A7M6
PRIDEiP0A7M6

Interactioni

Subunit structurei

Part of the 50s ribosomal subunit (PubMed:1092361, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:21499241, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts protein L23 (PubMed:2665813), trigger factor (PubMed:12226666) and protein nascent chains (PubMed:12756233). Might also contact SecE and probably does contact SecG when the SecYEG translocation complex is docked with the ribosome (PubMed:16292303).1 Publication13 Publications

Protein-protein interaction databases

DIPiDIP-47911N
IntActiP0A7M6, 35 interactors
STRINGi316385.ECDH10B_3487

Structurei

Secondary structure

163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A7M6
SMRiP0A7M6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7M6

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41083MP Bacteria
COG0255 LUCA
HOGENOMiHOG000248754
InParanoidiP0A7M6
KOiK02904
OMAiRFQNATN
PhylomeDBiP0A7M6

Family and domain databases

HAMAPiMF_00374 Ribosomal_L29, 1 hit
InterProiView protein in InterPro
IPR001854 Ribosomal_L29/L35
IPR036049 Ribosomal_L29/L35_sf
IPR018254 Ribosomal_L29_CS
PfamiView protein in Pfam
PF00831 Ribosomal_L29, 1 hit
SUPFAMiSSF46561 SSF46561, 1 hit
TIGRFAMsiTIGR00012 L29, 1 hit
PROSITEiView protein in PROSITE
PS00579 RIBOSOMAL_L29, 1 hit

Sequencei

Sequence statusi: Complete.

P0A7M6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAKELREKS VEELNTELLN LLREQFNLRM QAASGQLQQS HLLKQVRRDV
60
ARVKTLLNEK AGA
Length:63
Mass (Da):7,273
Last modified:April 1, 1988 - v1
Checksum:iDAEF8F126B0AA077
GO

Sequence cautioni

The sequence described in PubMed:1092361 differs from that shown. Exchange of two tryptic peptides.Curated

Mass spectrometryi

Molecular mass is 7273.4 Da from positions 1 - 63. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26468.1
U18997 Genomic DNA Translation: AAA58109.1
U00096 Genomic DNA Translation: AAC76337.1
AP009048 Genomic DNA Translation: BAE77979.1
PIRiB37519 R5EC29
RefSeqiNP_417771.1, NC_000913.3
WP_000644741.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76337; AAC76337; b3312
BAE77979; BAE77979; BAE77979
GeneIDi947807
KEGGiecj:JW3274
eco:b3312
PATRICifig|1411691.4.peg.3419

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26468.1
U18997 Genomic DNA Translation: AAA58109.1
U00096 Genomic DNA Translation: AAC76337.1
AP009048 Genomic DNA Translation: BAE77979.1
PIRiB37519 R5EC29
RefSeqiNP_417771.1, NC_000913.3
WP_000644741.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00w2-63[»]
2J28electron microscopy8.00X1-63[»]
2RDOelectron microscopy9.10X1-63[»]
2VRHelectron microscopy19.00D1-63[»]
3BBXelectron microscopy10.00X1-63[»]
3J45electron microscopy9.50Y1-63[»]
3J46electron microscopy10.10Y1-63[»]
3J5Lelectron microscopy6.60Y1-63[»]
3J7Zelectron microscopy3.90Y1-63[»]
3J8Gelectron microscopy5.0011-63[»]
3J9Yelectron microscopy3.90Y1-63[»]
3J9Zelectron microscopy3.60LW1-63[»]
3JA1electron microscopy3.60L01-63[»]
3JBUelectron microscopy3.6411-63[»]
3JBVelectron microscopy3.3211-63[»]
3JCDelectron microscopy3.70Y1-63[»]
3JCEelectron microscopy3.20Y1-63[»]
3JCJelectron microscopy3.70X1-63[»]
3JCNelectron microscopy4.60Y1-63[»]
4CSUelectron microscopy5.5011-63[»]
4U1UX-ray2.95BY/DY1-63[»]
4U1VX-ray3.00BY/DY1-63[»]
4U20X-ray2.90BY/DY1-63[»]
4U24X-ray2.90BY/DY1-63[»]
4U25X-ray2.90BY/DY1-63[»]
4U26X-ray2.80BY/DY1-63[»]
4U27X-ray2.80BY/DY1-63[»]
4UY8electron microscopy3.80Y1-63[»]
4V47electron microscopy12.30AW1-63[»]
4V48electron microscopy11.50AW1-63[»]
4V4HX-ray3.46BX/DX1-63[»]
4V4QX-ray3.46BX/DX1-63[»]
4V4Velectron microscopy15.00BW1-60[»]
4V4Welectron microscopy15.00BW1-60[»]
4V50X-ray3.22BY/DY1-63[»]
4V52X-ray3.21BX/DX1-63[»]
4V53X-ray3.54BX/DX1-63[»]
4V54X-ray3.30BX/DX1-63[»]
4V55X-ray4.00BX/DX1-63[»]
4V56X-ray3.93BX/DX1-63[»]
4V57X-ray3.50BX/DX1-63[»]
4V5BX-ray3.74AX/CX1-63[»]
4V5Helectron microscopy5.80B11-63[»]
4V5YX-ray4.45BX/DX1-63[»]
4V64X-ray3.50BX/DX1-63[»]
4V65electron microscopy9.00BQ1-63[»]
4V66electron microscopy9.00BQ1-63[»]
4V69electron microscopy6.70BY1-63[»]
4V6CX-ray3.19BY/DY1-63[»]
4V6DX-ray3.81BY/DY1-63[»]
4V6EX-ray3.71BY/DY1-63[»]
4V6Kelectron microscopy8.25AZ1-63[»]
4V6Lelectron microscopy13.20BZ1-63[»]
4V6Melectron microscopy7.10BY1-63[»]
4V6Nelectron microscopy12.10A01-63[»]
4V6Oelectron microscopy14.70B01-63[»]
4V6Pelectron microscopy13.50B01-63[»]
4V6Qelectron microscopy11.50B01-63[»]
4V6Relectron microscopy11.50B01-63[»]
4V6Selectron microscopy13.10A01-63[»]
4V6Telectron microscopy8.30BY1-63[»]
4V6Velectron microscopy9.80B21-63[»]
4V6Yelectron microscopy12.00BY1-63[»]
4V6Zelectron microscopy12.00BY1-63[»]
4V70electron microscopy17.00BY1-63[»]
4V71electron microscopy20.00BY1-63[»]
4V72electron microscopy13.00BY1-63[»]
4V73electron microscopy15.00BY1-63[»]
4V74electron microscopy17.00BY1-63[»]
4V75electron microscopy12.00BY1-63[»]
4V76electron microscopy17.00BY1-63[»]
4V77electron microscopy17.00BY1-63[»]
4V78electron microscopy20.00BY1-63[»]
4V79electron microscopy15.00BY1-63[»]
4V7Aelectron microscopy9.00BY1-63[»]
4V7Belectron microscopy6.80BY1-63[»]
4V7Celectron microscopy7.60B11-63[»]
4V7Delectron microscopy7.60A21-63[»]
4V7Ielectron microscopy9.60AY1-63[»]
4V7SX-ray3.25BY/DY1-63[»]
4V7TX-ray3.19BY/DY1-63[»]
4V7UX-ray3.10BY/DY1-63[»]
4V7VX-ray3.29BY/DY1-63[»]
4V85X-ray3.2021-63[»]
4V89X-ray3.70B21-63[»]
4V9CX-ray3.30BY/DY1-63[»]
4V9DX-ray3.00CY/DY1-63[»]
4V9OX-ray2.90AY/CY/EY/GY1-63[»]
4V9PX-ray2.90AY/CY/EY/GY1-63[»]
4WF1X-ray3.09BY/DY1-63[»]
4WOIX-ray3.00BY/CY1-63[»]
4WWWX-ray3.10RY/YY1-63[»]
4YBBX-ray2.10CZ/DZ2-63[»]
5ADYelectron microscopy4.50Y1-63[»]
5AFIelectron microscopy2.90Y1-63[»]
5AKAelectron microscopy5.70X1-63[»]
5GADelectron microscopy3.70Z1-63[»]
5GAEelectron microscopy3.33Z1-63[»]
5GAFelectron microscopy4.30Z2-63[»]
5GAGelectron microscopy3.80Z1-63[»]
5GAHelectron microscopy3.80Z1-63[»]
5H5Uelectron microscopy3.00Z1-63[»]
5IQRelectron microscopy3.00Y1-63[»]
5IT8X-ray3.12CZ/DZ2-63[»]
5J5BX-ray2.80CZ/DZ2-63[»]
5J7LX-ray3.00CZ/DZ2-63[»]
5J88X-ray3.32CZ/DZ2-63[»]
5J8AX-ray3.10CZ/DZ2-63[»]
5J91X-ray2.96CZ/DZ2-63[»]
5JC9X-ray3.03CZ/DZ2-63[»]
5JTEelectron microscopy3.60BY1-63[»]
5JU8electron microscopy3.60BY1-63[»]
5KCRelectron microscopy3.60121-63[»]
5KCSelectron microscopy3.90121-63[»]
5KPSelectron microscopy3.90Y1-63[»]
5KPVelectron microscopy4.10X1-63[»]
5KPWelectron microscopy3.90X1-63[»]
5KPXelectron microscopy3.90X1-63[»]
5L3Pelectron microscopy3.7021-63[»]
5LZAelectron microscopy3.60Y1-63[»]
5LZBelectron microscopy5.30Y1-63[»]
5LZCelectron microscopy4.80Y1-63[»]
5LZDelectron microscopy3.40Y1-63[»]
5LZEelectron microscopy3.50Y1-63[»]
5LZFelectron microscopy4.60Y1-63[»]
5MDVelectron microscopy2.97Y1-63[»]
5MDWelectron microscopy3.06Y1-63[»]
5MDYelectron microscopy3.35Y1-63[»]
5MDZelectron microscopy3.10Y1-63[»]
5MGPelectron microscopy3.10Y1-63[»]
5NCOelectron microscopy4.80Z2-63[»]
5NP6electron microscopy3.60w1-63[»]
5NWYelectron microscopy2.93l1-63[»]
5O2Relectron microscopy3.40Y1-63[»]
5U4Ielectron microscopy3.50Z1-63[»]
5U9Felectron microscopy3.20271-63[»]
5U9Gelectron microscopy3.20271-63[»]
5UYKelectron microscopy3.90271-63[»]
5UYLelectron microscopy3.60271-63[»]
5UYMelectron microscopy3.20271-63[»]
5UYNelectron microscopy4.00271-63[»]
5UYPelectron microscopy3.90271-63[»]
5UYQelectron microscopy3.80271-63[»]
5WDTelectron microscopy3.00Y1-60[»]
5WE4electron microscopy3.10Y1-60[»]
5WE6electron microscopy3.40Y1-60[»]
5WFKelectron microscopy3.40Y1-60[»]
6BU8electron microscopy3.50271-63[»]
6ENFelectron microscopy3.20Y1-63[»]
6ENJelectron microscopy3.70Y1-63[»]
6ENUelectron microscopy3.10Y1-63[»]
6GBZelectron microscopy3.80Y1-63[»]
6GC0electron microscopy3.80Y1-63[»]
6GC4electron microscopy4.30Y1-63[»]
6GC6electron microscopy4.30Y1-63[»]
6GC7electron microscopy4.30Y1-63[»]
6GC8electron microscopy3.80Y1-63[»]
6GWTelectron microscopy3.80Y1-63[»]
6GXMelectron microscopy3.80Y1-63[»]
6GXNelectron microscopy3.90Y1-63[»]
6GXOelectron microscopy3.90Y1-63[»]
6GXPelectron microscopy4.40Y1-63[»]
ProteinModelPortaliP0A7M6
SMRiP0A7M6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47911N
IntActiP0A7M6, 35 interactors
STRINGi316385.ECDH10B_3487

Proteomic databases

EPDiP0A7M6
PaxDbiP0A7M6
PRIDEiP0A7M6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76337; AAC76337; b3312
BAE77979; BAE77979; BAE77979
GeneIDi947807
KEGGiecj:JW3274
eco:b3312
PATRICifig|1411691.4.peg.3419

Organism-specific databases

EchoBASEiEB0880
EcoGeneiEG10887 rpmC

Phylogenomic databases

eggNOGiENOG41083MP Bacteria
COG0255 LUCA
HOGENOMiHOG000248754
InParanoidiP0A7M6
KOiK02904
OMAiRFQNATN
PhylomeDBiP0A7M6

Enzyme and pathway databases

BioCyciEcoCyc:EG10887-MONOMER
MetaCyc:EG10887-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7M6
PROiPR:P0A7M6

Family and domain databases

HAMAPiMF_00374 Ribosomal_L29, 1 hit
InterProiView protein in InterPro
IPR001854 Ribosomal_L29/L35
IPR036049 Ribosomal_L29/L35_sf
IPR018254 Ribosomal_L29_CS
PfamiView protein in Pfam
PF00831 Ribosomal_L29, 1 hit
SUPFAMiSSF46561 SSF46561, 1 hit
TIGRFAMsiTIGR00012 L29, 1 hit
PROSITEiView protein in PROSITE
PS00579 RIBOSOMAL_L29, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRL29_ECOLI
AccessioniPrimary (citable) accession number: P0A7M6
Secondary accession number(s): P02429, Q2M6X7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: October 10, 2018
This is version 132 of the entry and version 1 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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