Skip Header

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

50S ribosomal protein L2

Gene

rplB

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

Functioni

One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.6 Publications
In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.1 Publication

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-HAMAP
  • structural constituent of ribosome Source: GO_Central
  • transferase activity Source: InterPro
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10865-MONOMER.
ECOL316407:JW3279-MONOMER.
MetaCyc:EG10865-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Gene namesi
Name:rplB
Ordered Locus Names:b3317, JW3279
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10865. rplB.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230H → Q: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001295592 – 27350S ribosomal protein L2Add BLAST272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei242N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP60422.
PaxDbiP60422.
PRIDEiP60422.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Interacts weakly with S6 in one of the 3.5 A resolved structures.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaAP030044EBI-543515,EBI-548951
gspEP457592EBI-543515,EBI-1132437
metGP009592EBI-543515,EBI-909268
rpoAP0A7Z45EBI-543515,EBI-544985

Protein-protein interaction databases

BioGridi852132. 1 interactor.
DIPiDIP-35747N.
IntActiP60422. 362 interactors.
MINTiMINT-1322809.
STRINGi511145.b3317.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi8 – 10Combined sources3
Turni11 – 15Combined sources5
Beta strandi17 – 19Combined sources3
Beta strandi22 – 24Combined sources3
Helixi31 – 33Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi47 – 54Combined sources8
Beta strandi61 – 63Combined sources3
Beta strandi72 – 74Combined sources3
Beta strandi76 – 82Combined sources7
Beta strandi87 – 89Combined sources3
Beta strandi91 – 96Combined sources6
Turni97 – 99Combined sources3
Beta strandi100 – 105Combined sources6
Beta strandi107 – 109Combined sources3
Beta strandi112 – 115Combined sources4
Beta strandi118 – 121Combined sources4
Beta strandi125 – 127Combined sources3
Beta strandi129 – 131Combined sources3
Helixi132 – 134Combined sources3
Beta strandi140 – 147Combined sources8
Turni148 – 150Combined sources3
Beta strandi152 – 155Combined sources4
Beta strandi157 – 159Combined sources3
Beta strandi162 – 168Combined sources7
Beta strandi171 – 175Combined sources5
Beta strandi177 – 179Combined sources3
Beta strandi181 – 185Combined sources5
Beta strandi186 – 188Combined sources3
Beta strandi191 – 193Combined sources3
Helixi200 – 202Combined sources3
Helixi208 – 212Combined sources5
Turni213 – 215Combined sources3
Helixi222 – 224Combined sources3
Turni227 – 229Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi245 – 248Combined sources4
Beta strandi249 – 251Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi258 – 260Combined sources3
Turni261 – 266Combined sources6
Beta strandi267 – 269Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00C4-270[»]
2RDOelectron microscopy9.10C2-273[»]
3BBXelectron microscopy10.00C1-273[»]
3J5Lelectron microscopy6.60C2-272[»]
3J7Zelectron microscopy3.90C1-273[»]
3J8Gelectron microscopy5.00C1-273[»]
3J9Yelectron microscopy3.90C1-273[»]
3J9Zelectron microscopy3.60LN2-273[»]
3JA1electron microscopy3.60LD2-273[»]
3JBUelectron microscopy3.64c1-273[»]
3JBVelectron microscopy3.32c1-273[»]
3JCDelectron microscopy3.70C1-273[»]
3JCEelectron microscopy3.20C1-273[»]
3JCJelectron microscopy3.70B1-273[»]
3JCNelectron microscopy4.60C1-273[»]
487Delectron microscopy7.50I62-172[»]
4CSUelectron microscopy5.50C2-273[»]
4U1UX-ray2.95BC/DC2-272[»]
4U1VX-ray3.00BC/DC2-272[»]
4U20X-ray2.90BC/DC2-272[»]
4U24X-ray2.90BC/DC2-272[»]
4U25X-ray2.90BC/DC2-272[»]
4U26X-ray2.80BC/DC2-272[»]
4U27X-ray2.80BC/DC2-272[»]
4UY8electron microscopy3.80C2-272[»]
4V47electron microscopy12.30AA2-273[»]
4V48electron microscopy11.50AA2-273[»]
4V4HX-ray3.46BC/DC1-273[»]
4V4QX-ray3.46BC/DC1-273[»]
4V4Velectron microscopy15.00BA39-265[»]
4V4Welectron microscopy15.00BA39-265[»]
4V50X-ray3.22BC/DC2-273[»]
4V52X-ray3.21BC/DC2-273[»]
4V53X-ray3.54BC/DC2-273[»]
4V54X-ray3.30BC/DC2-273[»]
4V55X-ray4.00BC/DC2-273[»]
4V56X-ray3.93BC/DC2-273[»]
4V57X-ray3.50BC/DC2-273[»]
4V5BX-ray3.74AC/CC1-273[»]
4V5Helectron microscopy5.80BC2-272[»]
4V5YX-ray4.45BC/DC2-273[»]
4V64X-ray3.50BC/DC1-273[»]
4V65electron microscopy9.00BN1-270[»]
4V66electron microscopy9.00BN1-270[»]
4V69electron microscopy6.70BC2-272[»]
4V6CX-ray3.19BC/DC1-273[»]
4V6DX-ray3.81BC/DC1-273[»]
4V6EX-ray3.71BC/DC1-273[»]
4V6Kelectron microscopy8.25AD1-273[»]
4V6Lelectron microscopy13.20BD1-273[»]
4V6Melectron microscopy7.10B62-273[»]
4V6Nelectron microscopy12.10AD2-273[»]
4V6Oelectron microscopy14.70BD2-273[»]
4V6Pelectron microscopy13.50BD2-273[»]
4V6Qelectron microscopy11.50BD2-273[»]
4V6Relectron microscopy11.50BD2-273[»]
4V6Selectron microscopy13.10AD2-273[»]
4V6Telectron microscopy8.30BC2-272[»]
4V6Velectron microscopy9.80BD2-273[»]
4V6Yelectron microscopy12.00BC1-272[»]
4V6Zelectron microscopy12.00BC1-272[»]
4V70electron microscopy17.00BC1-272[»]
4V71electron microscopy20.00BC1-272[»]
4V72electron microscopy13.00BC1-272[»]
4V73electron microscopy15.00BC1-272[»]
4V74electron microscopy17.00BC1-272[»]
4V75electron microscopy12.00BC1-272[»]
4V76electron microscopy17.00BC1-272[»]
4V77electron microscopy17.00BC1-272[»]
4V78electron microscopy20.00BC1-272[»]
4V79electron microscopy15.00BC1-272[»]
4V7Aelectron microscopy9.00BC1-272[»]
4V7Belectron microscopy6.80BC1-273[»]
4V7Celectron microscopy7.60BD2-273[»]
4V7Delectron microscopy7.60AD2-273[»]
4V7Ielectron microscopy9.60A61-273[»]
4V7SX-ray3.25BC/DC2-272[»]
4V7TX-ray3.19BC/DC2-272[»]
4V7UX-ray3.10BC/DC2-272[»]
4V7VX-ray3.29BC/DC2-272[»]
4V85X-ray3.20C1-273[»]
4V89X-ray3.70BC1-273[»]
4V9CX-ray3.30BC/DC1-273[»]
4V9DX-ray3.00CC/DC2-272[»]
4V9OX-ray2.90AC/CC/EC/GC1-273[»]
4V9PX-ray2.90AC/CC/EC/GC1-273[»]
4WF1X-ray3.09BC/DC2-272[»]
4WOIX-ray3.00BC/CC1-273[»]
4WWWX-ray3.10RC/YC2-272[»]
4YBBX-ray2.10CC/DC2-272[»]
5ADYelectron microscopy4.50C1-273[»]
5AFIelectron microscopy2.90C1-273[»]
5AKAelectron microscopy5.70C1-273[»]
5GADelectron microscopy3.70C1-273[»]
5GAEelectron microscopy3.33C1-273[»]
5GAFelectron microscopy4.30C2-272[»]
5GAGelectron microscopy3.80C1-273[»]
5GAHelectron microscopy3.80C1-273[»]
5IQRelectron microscopy3.00B1-273[»]
5IT8X-ray3.12CC/DC2-272[»]
5J5BX-ray2.80CC/DC2-272[»]
5J7LX-ray3.00CC/DC2-272[»]
5J88X-ray3.32CC/DC2-273[»]
5J8AX-ray3.10CC/DC2-273[»]
5J91X-ray2.96CC/DC2-273[»]
5JC9X-ray3.03CC/DC2-272[»]
5JTEelectron microscopy3.60BC1-273[»]
5JU8electron microscopy3.60BC1-273[»]
5KCRelectron microscopy3.601D1-273[»]
5KCSelectron microscopy3.901D1-273[»]
5KPSelectron microscopy3.90B1-273[»]
5KPVelectron microscopy4.10A1-273[»]
5KPWelectron microscopy3.90A1-273[»]
5KPXelectron microscopy3.90A1-273[»]
5L3Pelectron microscopy3.70D1-273[»]
ProteinModelPortaliP60422.
SMRiP60422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60422.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiENOG4105CFD. Bacteria.
COG0090. LUCA.
HOGENOMiHOG000232982.
InParanoidiP60422.
KOiK02886.
OMAiPIKAGNN.
PhylomeDBiP60422.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_B. Ribosomal_L2_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT
60 70 80 90 100
TRHIGGGHKQ AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE
110 120 130 140 150
RRYILAPKGL KAGDQIQSGV DAAIKPGNTL PMRNIPVGST VHNVEMKPGK
160 170 180 190 200
GGQLARSAGT YVQIVARDGA YVTLRLRSGE MRKVEADCRA TLGEVGNAEH
210 220 230 240 250
MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF GKHPVTPWGV
260 270
QTKGKKTRSN KRTDKFIVRR RSK
Length:273
Mass (Da):29,860
Last modified:January 23, 2007 - v2
Checksum:i1010BDE8D8C68B9B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti232 – 235HGGG → GGGH AA sequence (Ref. 4) Curated4

Mass spectrometryi

Molecular mass is 29732.3 Da from positions 2 - 273. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26463.1.
U18997 Genomic DNA. Translation: AAA58114.1.
U00096 Genomic DNA. Translation: AAC76342.1.
AP009048 Genomic DNA. Translation: BAE77974.1.
PIRiE23129. R5EC2.
RefSeqiNP_417776.1. NC_000913.3.
WP_000301864.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76342; AAC76342; b3317.
BAE77974; BAE77974; BAE77974.
GeneIDi5548832.
947820.
KEGGiecj:JW3279.
eco:b3317.
PATRICi32122066. VBIEscCol129921_3410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26463.1.
U18997 Genomic DNA. Translation: AAA58114.1.
U00096 Genomic DNA. Translation: AAC76342.1.
AP009048 Genomic DNA. Translation: BAE77974.1.
PIRiE23129. R5EC2.
RefSeqiNP_417776.1. NC_000913.3.
WP_000301864.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00C4-270[»]
2RDOelectron microscopy9.10C2-273[»]
3BBXelectron microscopy10.00C1-273[»]
3J5Lelectron microscopy6.60C2-272[»]
3J7Zelectron microscopy3.90C1-273[»]
3J8Gelectron microscopy5.00C1-273[»]
3J9Yelectron microscopy3.90C1-273[»]
3J9Zelectron microscopy3.60LN2-273[»]
3JA1electron microscopy3.60LD2-273[»]
3JBUelectron microscopy3.64c1-273[»]
3JBVelectron microscopy3.32c1-273[»]
3JCDelectron microscopy3.70C1-273[»]
3JCEelectron microscopy3.20C1-273[»]
3JCJelectron microscopy3.70B1-273[»]
3JCNelectron microscopy4.60C1-273[»]
487Delectron microscopy7.50I62-172[»]
4CSUelectron microscopy5.50C2-273[»]
4U1UX-ray2.95BC/DC2-272[»]
4U1VX-ray3.00BC/DC2-272[»]
4U20X-ray2.90BC/DC2-272[»]
4U24X-ray2.90BC/DC2-272[»]
4U25X-ray2.90BC/DC2-272[»]
4U26X-ray2.80BC/DC2-272[»]
4U27X-ray2.80BC/DC2-272[»]
4UY8electron microscopy3.80C2-272[»]
4V47electron microscopy12.30AA2-273[»]
4V48electron microscopy11.50AA2-273[»]
4V4HX-ray3.46BC/DC1-273[»]
4V4QX-ray3.46BC/DC1-273[»]
4V4Velectron microscopy15.00BA39-265[»]
4V4Welectron microscopy15.00BA39-265[»]
4V50X-ray3.22BC/DC2-273[»]
4V52X-ray3.21BC/DC2-273[»]
4V53X-ray3.54BC/DC2-273[»]
4V54X-ray3.30BC/DC2-273[»]
4V55X-ray4.00BC/DC2-273[»]
4V56X-ray3.93BC/DC2-273[»]
4V57X-ray3.50BC/DC2-273[»]
4V5BX-ray3.74AC/CC1-273[»]
4V5Helectron microscopy5.80BC2-272[»]
4V5YX-ray4.45BC/DC2-273[»]
4V64X-ray3.50BC/DC1-273[»]
4V65electron microscopy9.00BN1-270[»]
4V66electron microscopy9.00BN1-270[»]
4V69electron microscopy6.70BC2-272[»]
4V6CX-ray3.19BC/DC1-273[»]
4V6DX-ray3.81BC/DC1-273[»]
4V6EX-ray3.71BC/DC1-273[»]
4V6Kelectron microscopy8.25AD1-273[»]
4V6Lelectron microscopy13.20BD1-273[»]
4V6Melectron microscopy7.10B62-273[»]
4V6Nelectron microscopy12.10AD2-273[»]
4V6Oelectron microscopy14.70BD2-273[»]
4V6Pelectron microscopy13.50BD2-273[»]
4V6Qelectron microscopy11.50BD2-273[»]
4V6Relectron microscopy11.50BD2-273[»]
4V6Selectron microscopy13.10AD2-273[»]
4V6Telectron microscopy8.30BC2-272[»]
4V6Velectron microscopy9.80BD2-273[»]
4V6Yelectron microscopy12.00BC1-272[»]
4V6Zelectron microscopy12.00BC1-272[»]
4V70electron microscopy17.00BC1-272[»]
4V71electron microscopy20.00BC1-272[»]
4V72electron microscopy13.00BC1-272[»]
4V73electron microscopy15.00BC1-272[»]
4V74electron microscopy17.00BC1-272[»]
4V75electron microscopy12.00BC1-272[»]
4V76electron microscopy17.00BC1-272[»]
4V77electron microscopy17.00BC1-272[»]
4V78electron microscopy20.00BC1-272[»]
4V79electron microscopy15.00BC1-272[»]
4V7Aelectron microscopy9.00BC1-272[»]
4V7Belectron microscopy6.80BC1-273[»]
4V7Celectron microscopy7.60BD2-273[»]
4V7Delectron microscopy7.60AD2-273[»]
4V7Ielectron microscopy9.60A61-273[»]
4V7SX-ray3.25BC/DC2-272[»]
4V7TX-ray3.19BC/DC2-272[»]
4V7UX-ray3.10BC/DC2-272[»]
4V7VX-ray3.29BC/DC2-272[»]
4V85X-ray3.20C1-273[»]
4V89X-ray3.70BC1-273[»]
4V9CX-ray3.30BC/DC1-273[»]
4V9DX-ray3.00CC/DC2-272[»]
4V9OX-ray2.90AC/CC/EC/GC1-273[»]
4V9PX-ray2.90AC/CC/EC/GC1-273[»]
4WF1X-ray3.09BC/DC2-272[»]
4WOIX-ray3.00BC/CC1-273[»]
4WWWX-ray3.10RC/YC2-272[»]
4YBBX-ray2.10CC/DC2-272[»]
5ADYelectron microscopy4.50C1-273[»]
5AFIelectron microscopy2.90C1-273[»]
5AKAelectron microscopy5.70C1-273[»]
5GADelectron microscopy3.70C1-273[»]
5GAEelectron microscopy3.33C1-273[»]
5GAFelectron microscopy4.30C2-272[»]
5GAGelectron microscopy3.80C1-273[»]
5GAHelectron microscopy3.80C1-273[»]
5IQRelectron microscopy3.00B1-273[»]
5IT8X-ray3.12CC/DC2-272[»]
5J5BX-ray2.80CC/DC2-272[»]
5J7LX-ray3.00CC/DC2-272[»]
5J88X-ray3.32CC/DC2-273[»]
5J8AX-ray3.10CC/DC2-273[»]
5J91X-ray2.96CC/DC2-273[»]
5JC9X-ray3.03CC/DC2-272[»]
5JTEelectron microscopy3.60BC1-273[»]
5JU8electron microscopy3.60BC1-273[»]
5KCRelectron microscopy3.601D1-273[»]
5KCSelectron microscopy3.901D1-273[»]
5KPSelectron microscopy3.90B1-273[»]
5KPVelectron microscopy4.10A1-273[»]
5KPWelectron microscopy3.90A1-273[»]
5KPXelectron microscopy3.90A1-273[»]
5L3Pelectron microscopy3.70D1-273[»]
ProteinModelPortaliP60422.
SMRiP60422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852132. 1 interactor.
DIPiDIP-35747N.
IntActiP60422. 362 interactors.
MINTiMINT-1322809.
STRINGi511145.b3317.

Proteomic databases

EPDiP60422.
PaxDbiP60422.
PRIDEiP60422.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76342; AAC76342; b3317.
BAE77974; BAE77974; BAE77974.
GeneIDi5548832.
947820.
KEGGiecj:JW3279.
eco:b3317.
PATRICi32122066. VBIEscCol129921_3410.

Organism-specific databases

EchoBASEiEB0858.
EcoGeneiEG10865. rplB.

Phylogenomic databases

eggNOGiENOG4105CFD. Bacteria.
COG0090. LUCA.
HOGENOMiHOG000232982.
InParanoidiP60422.
KOiK02886.
OMAiPIKAGNN.
PhylomeDBiP60422.

Enzyme and pathway databases

BioCyciEcoCyc:EG10865-MONOMER.
ECOL316407:JW3279-MONOMER.
MetaCyc:EG10865-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60422.
PROiP60422.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_B. Ribosomal_L2_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL2_ECOLI
AccessioniPrimary (citable) accession number: P60422
Secondary accession number(s): P02387, Q2M6Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein can be partially replaced in vivo by its H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome) homolog.1 Publication

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.