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Protein

50S ribosomal protein L28

Gene

rpmB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10886-MONOMER.
ECOL316407:JW3612-MONOMER.
MetaCyc:EG10886-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L28
Gene namesi
Name:rpmB
Ordered Locus Names:b3637, JW3612
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10886. rpmB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001784682 – 7850S ribosomal protein L28Add BLAST77

Proteomic databases

EPDiP0A7M2.
PaxDbiP0A7M2.
PRIDEiP0A7M2.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rpmFP0A7N42EBI-543024,EBI-1112732

Protein-protein interaction databases

BioGridi4262565. 94 interactors.
851280. 1 interactor.
DIPiDIP-35745N.
IntActiP0A7M2. 113 interactors.
MINTiMINT-1306660.
STRINGi511145.b3637.

Structurei

Secondary structure

178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 8Combined sources3
Beta strandi13 – 16Combined sources4
Helixi20 – 22Combined sources3
Beta strandi26 – 29Combined sources4
Beta strandi33 – 40Combined sources8
Helixi41 – 43Combined sources3
Beta strandi45 – 52Combined sources8
Helixi53 – 62Combined sources10
Helixi64 – 73Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J5Lelectron microscopy6.60X2-78[»]
3J7Zelectron microscopy3.90X1-78[»]
3J8Gelectron microscopy5.0001-78[»]
3J9Yelectron microscopy3.90X1-78[»]
3J9Zelectron microscopy3.60LV2-78[»]
3JA1electron microscopy3.60LZ2-78[»]
3JBUelectron microscopy3.6401-78[»]
3JBVelectron microscopy3.3201-78[»]
3JCDelectron microscopy3.70X1-78[»]
3JCEelectron microscopy3.20X1-78[»]
3JCJelectron microscopy3.70W1-78[»]
3JCNelectron microscopy4.60X1-78[»]
4CSUelectron microscopy5.5002-78[»]
4U1UX-ray2.95BX/DX2-78[»]
4U1VX-ray3.00BX/DX2-78[»]
4U20X-ray2.90BX/DX2-78[»]
4U24X-ray2.90BX/DX2-78[»]
4U25X-ray2.90BX/DX2-78[»]
4U26X-ray2.80BX/DX2-78[»]
4U27X-ray2.80BX/DX2-78[»]
4UY8electron microscopy3.80X2-78[»]
4V50X-ray3.22BX/DX2-78[»]
4V52X-ray3.21BZ/DZ1-78[»]
4V53X-ray3.54BZ/DZ1-78[»]
4V54X-ray3.30BZ/DZ1-78[»]
4V55X-ray4.00BZ/DZ1-78[»]
4V56X-ray3.93BZ/DZ1-78[»]
4V57X-ray3.50BZ/DZ1-78[»]
4V5Helectron microscopy5.80B02-78[»]
4V5YX-ray4.45BZ/DZ1-78[»]
4V64X-ray3.50BZ/DZ1-78[»]
4V69electron microscopy6.70BX2-78[»]
4V6CX-ray3.19BX/DX1-78[»]
4V6DX-ray3.81BX/DX1-78[»]
4V6EX-ray3.71BX/DX1-78[»]
4V6Kelectron microscopy8.25AY1-78[»]
4V6Lelectron microscopy13.20BY1-78[»]
4V6Melectron microscopy7.10BX2-78[»]
4V6Nelectron microscopy12.10AZ2-78[»]
4V6Oelectron microscopy14.70BZ2-78[»]
4V6Pelectron microscopy13.50BZ2-78[»]
4V6Qelectron microscopy11.50BZ2-78[»]
4V6Relectron microscopy11.50BZ2-78[»]
4V6Selectron microscopy13.10AZ2-78[»]
4V6Telectron microscopy8.30BX2-78[»]
4V6Velectron microscopy9.80B12-78[»]
4V6Yelectron microscopy12.00BX1-78[»]
4V6Zelectron microscopy12.00BX1-78[»]
4V70electron microscopy17.00BX1-78[»]
4V71electron microscopy20.00BX1-78[»]
4V72electron microscopy13.00BX1-78[»]
4V73electron microscopy15.00BX1-78[»]
4V74electron microscopy17.00BX1-78[»]
4V75electron microscopy12.00BX1-78[»]
4V76electron microscopy17.00BX1-78[»]
4V77electron microscopy17.00BX1-78[»]
4V78electron microscopy20.00BX1-78[»]
4V79electron microscopy15.00BX1-78[»]
4V7Aelectron microscopy9.00BX1-78[»]
4V7Belectron microscopy6.80BX1-78[»]
4V7Celectron microscopy7.60BZ2-78[»]
4V7Delectron microscopy7.60A12-78[»]
4V7Ielectron microscopy9.60AX1-78[»]
4V7SX-ray3.25BX/DX2-78[»]
4V7TX-ray3.19BX/DX2-78[»]
4V7UX-ray3.10BX/DX2-78[»]
4V7VX-ray3.29BX/DX2-78[»]
4V85X-ray3.2011-78[»]
4V89X-ray3.70B11-78[»]
4V9CX-ray3.30BX/DX1-78[»]
4V9DX-ray3.00CX/DX2-78[»]
4V9OX-ray2.90AX/CX/EX/GX1-78[»]
4V9PX-ray2.90AX/CX/EX/GX1-78[»]
4WF1X-ray3.09BX/DX2-78[»]
4WOIX-ray3.00BX/CX1-78[»]
4WWWX-ray3.10RX/YX2-78[»]
4YBBX-ray2.10CY/DY2-78[»]
5ADYelectron microscopy4.50X1-78[»]
5AFIelectron microscopy2.90X1-78[»]
5GADelectron microscopy3.70Y1-78[»]
5GAEelectron microscopy3.33Y1-78[»]
5GAFelectron microscopy4.30Y2-78[»]
5GAGelectron microscopy3.80Y1-78[»]
5GAHelectron microscopy3.80Y1-78[»]
5IQRelectron microscopy3.00X1-78[»]
5IT8X-ray3.12CY/DY2-78[»]
5J5BX-ray2.80CY/DY2-78[»]
5J7LX-ray3.00CY/DY2-78[»]
5J88X-ray3.32CY/DY2-78[»]
5J8AX-ray3.10CY/DY2-78[»]
5J91X-ray2.96CY/DY2-78[»]
5JC9X-ray3.03CY/DY2-78[»]
5JTEelectron microscopy3.60BX1-78[»]
5JU8electron microscopy3.60BX1-78[»]
5KCRelectron microscopy3.60111-78[»]
5KCSelectron microscopy3.90111-78[»]
5KPSelectron microscopy3.90X1-78[»]
5KPVelectron microscopy4.10W1-78[»]
5KPWelectron microscopy3.90W1-78[»]
5KPXelectron microscopy3.90W1-78[»]
5L3Pelectron microscopy3.7011-78[»]
ProteinModelPortaliP0A7M2.
SMRiP0A7M2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7M2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L28P family.Curated

Phylogenomic databases

eggNOGiENOG4105KDC. Bacteria.
COG0227. LUCA.
HOGENOMiHOG000040462.
InParanoidiP0A7M2.
KOiK02902.
OMAiWLPSERR.
PhylomeDBiP0A7M2.

Family and domain databases

HAMAPiMF_00373. Ribosomal_L28. 1 hit.
InterProiIPR026569. Ribo_L28/L24.
IPR001383. Ribosomal_L28.
[Graphical view]
PANTHERiPTHR13528. PTHR13528. 1 hit.
PfamiPF00830. Ribosomal_L28. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00009. L28. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A7M2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVCQVTGK RPVTGNNRSH ALNATKRRFL PNLHSHRFWV ESEKRFVTLR
60 70
VSAKGMRVID KKGIDTVLAE LRARGEKY
Length:78
Mass (Da):9,006
Last modified:January 23, 2007 - v2
Checksum:i2616ADB10772A57C
GO

Mass spectrometryi

Molecular mass is 8875.0 Da from positions 2 - 78. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01677 Genomic DNA. Translation: AAA74099.1.
L10328 Genomic DNA. Translation: AAA61990.1.
U00096 Genomic DNA. Translation: AAC76661.1.
AP009048 Genomic DNA. Translation: BAE77655.1.
PIRiS42443. R5EC28.
RefSeqiNP_418094.1. NC_000913.3.
WP_000091955.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76661; AAC76661; b3637.
BAE77655; BAE77655; BAE77655.
GeneIDi946941.
KEGGiecj:JW3612.
eco:b3637.
PATRICi32122761. VBIEscCol129921_3757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01677 Genomic DNA. Translation: AAA74099.1.
L10328 Genomic DNA. Translation: AAA61990.1.
U00096 Genomic DNA. Translation: AAC76661.1.
AP009048 Genomic DNA. Translation: BAE77655.1.
PIRiS42443. R5EC28.
RefSeqiNP_418094.1. NC_000913.3.
WP_000091955.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J5Lelectron microscopy6.60X2-78[»]
3J7Zelectron microscopy3.90X1-78[»]
3J8Gelectron microscopy5.0001-78[»]
3J9Yelectron microscopy3.90X1-78[»]
3J9Zelectron microscopy3.60LV2-78[»]
3JA1electron microscopy3.60LZ2-78[»]
3JBUelectron microscopy3.6401-78[»]
3JBVelectron microscopy3.3201-78[»]
3JCDelectron microscopy3.70X1-78[»]
3JCEelectron microscopy3.20X1-78[»]
3JCJelectron microscopy3.70W1-78[»]
3JCNelectron microscopy4.60X1-78[»]
4CSUelectron microscopy5.5002-78[»]
4U1UX-ray2.95BX/DX2-78[»]
4U1VX-ray3.00BX/DX2-78[»]
4U20X-ray2.90BX/DX2-78[»]
4U24X-ray2.90BX/DX2-78[»]
4U25X-ray2.90BX/DX2-78[»]
4U26X-ray2.80BX/DX2-78[»]
4U27X-ray2.80BX/DX2-78[»]
4UY8electron microscopy3.80X2-78[»]
4V50X-ray3.22BX/DX2-78[»]
4V52X-ray3.21BZ/DZ1-78[»]
4V53X-ray3.54BZ/DZ1-78[»]
4V54X-ray3.30BZ/DZ1-78[»]
4V55X-ray4.00BZ/DZ1-78[»]
4V56X-ray3.93BZ/DZ1-78[»]
4V57X-ray3.50BZ/DZ1-78[»]
4V5Helectron microscopy5.80B02-78[»]
4V5YX-ray4.45BZ/DZ1-78[»]
4V64X-ray3.50BZ/DZ1-78[»]
4V69electron microscopy6.70BX2-78[»]
4V6CX-ray3.19BX/DX1-78[»]
4V6DX-ray3.81BX/DX1-78[»]
4V6EX-ray3.71BX/DX1-78[»]
4V6Kelectron microscopy8.25AY1-78[»]
4V6Lelectron microscopy13.20BY1-78[»]
4V6Melectron microscopy7.10BX2-78[»]
4V6Nelectron microscopy12.10AZ2-78[»]
4V6Oelectron microscopy14.70BZ2-78[»]
4V6Pelectron microscopy13.50BZ2-78[»]
4V6Qelectron microscopy11.50BZ2-78[»]
4V6Relectron microscopy11.50BZ2-78[»]
4V6Selectron microscopy13.10AZ2-78[»]
4V6Telectron microscopy8.30BX2-78[»]
4V6Velectron microscopy9.80B12-78[»]
4V6Yelectron microscopy12.00BX1-78[»]
4V6Zelectron microscopy12.00BX1-78[»]
4V70electron microscopy17.00BX1-78[»]
4V71electron microscopy20.00BX1-78[»]
4V72electron microscopy13.00BX1-78[»]
4V73electron microscopy15.00BX1-78[»]
4V74electron microscopy17.00BX1-78[»]
4V75electron microscopy12.00BX1-78[»]
4V76electron microscopy17.00BX1-78[»]
4V77electron microscopy17.00BX1-78[»]
4V78electron microscopy20.00BX1-78[»]
4V79electron microscopy15.00BX1-78[»]
4V7Aelectron microscopy9.00BX1-78[»]
4V7Belectron microscopy6.80BX1-78[»]
4V7Celectron microscopy7.60BZ2-78[»]
4V7Delectron microscopy7.60A12-78[»]
4V7Ielectron microscopy9.60AX1-78[»]
4V7SX-ray3.25BX/DX2-78[»]
4V7TX-ray3.19BX/DX2-78[»]
4V7UX-ray3.10BX/DX2-78[»]
4V7VX-ray3.29BX/DX2-78[»]
4V85X-ray3.2011-78[»]
4V89X-ray3.70B11-78[»]
4V9CX-ray3.30BX/DX1-78[»]
4V9DX-ray3.00CX/DX2-78[»]
4V9OX-ray2.90AX/CX/EX/GX1-78[»]
4V9PX-ray2.90AX/CX/EX/GX1-78[»]
4WF1X-ray3.09BX/DX2-78[»]
4WOIX-ray3.00BX/CX1-78[»]
4WWWX-ray3.10RX/YX2-78[»]
4YBBX-ray2.10CY/DY2-78[»]
5ADYelectron microscopy4.50X1-78[»]
5AFIelectron microscopy2.90X1-78[»]
5GADelectron microscopy3.70Y1-78[»]
5GAEelectron microscopy3.33Y1-78[»]
5GAFelectron microscopy4.30Y2-78[»]
5GAGelectron microscopy3.80Y1-78[»]
5GAHelectron microscopy3.80Y1-78[»]
5IQRelectron microscopy3.00X1-78[»]
5IT8X-ray3.12CY/DY2-78[»]
5J5BX-ray2.80CY/DY2-78[»]
5J7LX-ray3.00CY/DY2-78[»]
5J88X-ray3.32CY/DY2-78[»]
5J8AX-ray3.10CY/DY2-78[»]
5J91X-ray2.96CY/DY2-78[»]
5JC9X-ray3.03CY/DY2-78[»]
5JTEelectron microscopy3.60BX1-78[»]
5JU8electron microscopy3.60BX1-78[»]
5KCRelectron microscopy3.60111-78[»]
5KCSelectron microscopy3.90111-78[»]
5KPSelectron microscopy3.90X1-78[»]
5KPVelectron microscopy4.10W1-78[»]
5KPWelectron microscopy3.90W1-78[»]
5KPXelectron microscopy3.90W1-78[»]
5L3Pelectron microscopy3.7011-78[»]
ProteinModelPortaliP0A7M2.
SMRiP0A7M2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262565. 94 interactors.
851280. 1 interactor.
DIPiDIP-35745N.
IntActiP0A7M2. 113 interactors.
MINTiMINT-1306660.
STRINGi511145.b3637.

Proteomic databases

EPDiP0A7M2.
PaxDbiP0A7M2.
PRIDEiP0A7M2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76661; AAC76661; b3637.
BAE77655; BAE77655; BAE77655.
GeneIDi946941.
KEGGiecj:JW3612.
eco:b3637.
PATRICi32122761. VBIEscCol129921_3757.

Organism-specific databases

EchoBASEiEB0879.
EcoGeneiEG10886. rpmB.

Phylogenomic databases

eggNOGiENOG4105KDC. Bacteria.
COG0227. LUCA.
HOGENOMiHOG000040462.
InParanoidiP0A7M2.
KOiK02902.
OMAiWLPSERR.
PhylomeDBiP0A7M2.

Enzyme and pathway databases

BioCyciEcoCyc:EG10886-MONOMER.
ECOL316407:JW3612-MONOMER.
MetaCyc:EG10886-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7M2.
PROiP0A7M2.

Family and domain databases

HAMAPiMF_00373. Ribosomal_L28. 1 hit.
InterProiIPR026569. Ribo_L28/L24.
IPR001383. Ribosomal_L28.
[Graphical view]
PANTHERiPTHR13528. PTHR13528. 1 hit.
PfamiPF00830. Ribosomal_L28. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00009. L28. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL28_ECOLI
AccessioniPrimary (citable) accession number: P0A7M2
Secondary accession number(s): P02428, Q2M7V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.