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P0AA10

- RL13_ECOLI

UniProt

P0AA10 - RL13_ECOLI

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Protein

50S ribosomal protein L13

Gene
rplM, b3231, JW3200
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.UniRule annotation

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro
  2. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10874-MONOMER.
ECOL316407:JW3200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L13
Gene namesi
Name:rplM
Ordered Locus Names:b3231, JW3200
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10874. rplM.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14214250S ribosomal protein L13UniRule annotationPRO_0000133734Add
BLAST

Proteomic databases

PaxDbiP0AA10.
PRIDEiP0AA10.

Expressioni

Gene expression databases

GenevestigatoriP0AA10.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.1 Publication

Protein-protein interaction databases

BioGridi852140. 1 interaction.
DIPiDIP-47837N.
IntActiP0AA10. 112 interactions.
MINTiMINT-1269598.
STRINGi511145.b3231.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103
Beta strandi16 – 194
Beta strandi21 – 233
Helixi27 – 3711
Turni38 – 403
Beta strandi42 – 443
Beta strandi46 – 483
Beta strandi54 – 574
Helixi59 – 613
Beta strandi65 – 673
Helixi68 – 714
Beta strandi75 – 773
Beta strandi79 – 824
Beta strandi84 – 863
Helixi89 – 946
Helixi99 – 1068
Helixi113 – 1197
Beta strandi122 – 1243
Beta strandi126 – 1283
Helixi133 – 1353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00m1-142[»]
1P85electron microscopy12.30H1-142[»]
1P86electron microscopy11.50H1-142[»]
1VS6X-ray3.46J1-142[»]
1VS8X-ray3.46J1-142[»]
1VT2X-ray3.30J1-142[»]
2AW4X-ray3.46J1-142[»]
2AWBX-ray3.46J1-142[»]
2GYAelectron microscopy15.00H1-142[»]
2GYCelectron microscopy15.00H1-142[»]
2I2TX-ray3.22J1-142[»]
2I2VX-ray3.22J1-142[»]
2J28electron microscopy8.00J1-140[»]
2QAMX-ray3.21J1-142[»]
2QAOX-ray3.21J1-142[»]
2QBAX-ray3.54J1-142[»]
2QBCX-ray3.54J1-142[»]
2QBEX-ray3.30J1-142[»]
2QBGX-ray3.30J1-142[»]
2QBIX-ray4.00J1-142[»]
2QBKX-ray4.00J1-142[»]
2QOVX-ray3.93J1-142[»]
2QOXX-ray3.93J1-142[»]
2QOZX-ray3.50J1-142[»]
2QP1X-ray3.50J1-142[»]
2RDOelectron microscopy9.10J1-142[»]
2WWQelectron microscopy5.80J1-142[»]
2Z4LX-ray4.45J1-142[»]
2Z4NX-ray4.45J1-142[»]
3BBXelectron microscopy10.00J1-142[»]
3E1Belectron microscopy-61-140[»]
3E1Delectron microscopy-61-140[»]
3FIKelectron microscopy6.70J1-142[»]
3I1NX-ray3.19J1-142[»]
3I1PX-ray3.19J1-142[»]
3I1RX-ray3.81J1-142[»]
3I1TX-ray3.81J1-142[»]
3I20X-ray3.71J1-142[»]
3I22X-ray3.71J1-142[»]
3IY9electron microscopy14.10J1-140[»]
3IZTelectron microscopy-K1-142[»]
3IZUelectron microscopy-K1-142[»]
3J01electron microscopy-J1-142[»]
3J0Telectron microscopy12.10L1-142[»]
3J0Welectron microscopy14.70L1-142[»]
3J0Yelectron microscopy13.50L1-142[»]
3J11electron microscopy13.10L1-142[»]
3J12electron microscopy11.50L1-142[»]
3J14electron microscopy11.50L1-142[»]
3J19electron microscopy8.30J1-142[»]
3J37electron microscopy9.80N1-142[»]
3J4Xelectron microscopy12.00J1-142[»]
3J50electron microscopy20.00J1-142[»]
3J51electron microscopy17.00J1-142[»]
3J52electron microscopy12.00J1-142[»]
3J54electron microscopy13.00J1-142[»]
3J56electron microscopy15.00J1-142[»]
3J58electron microscopy17.00J1-142[»]
3J5Aelectron microscopy12.00J1-142[»]
3J5Celectron microscopy17.00J1-142[»]
3J5Eelectron microscopy17.00J1-142[»]
3J5Gelectron microscopy20.00J1-142[»]
3J5Ielectron microscopy15.00J1-142[»]
3J5Kelectron microscopy9.00J1-142[»]
3J5Lelectron microscopy6.60J1-142[»]
3J5Oelectron microscopy6.80J1-142[»]
3J5Uelectron microscopy7.60L1-142[»]
3J5Welectron microscopy7.60M1-142[»]
3KCRelectron microscopy-J1-142[»]
3OASX-ray3.25J1-142[»]
3OATX-ray3.25J1-142[»]
3OFCX-ray3.19J1-142[»]
3OFDX-ray3.19J1-142[»]
3OFQX-ray3.10J1-142[»]
3OFRX-ray3.10J1-142[»]
3OFZX-ray3.29J1-142[»]
3OG0X-ray3.29J1-142[»]
3ORBX-ray3.30J1-142[»]
3R8SX-ray3.00J1-142[»]
3R8TX-ray3.00J1-142[»]
3SGFX-ray3.20N1-142[»]
3UOSX-ray3.70N1-142[»]
4CSUelectron microscopy5.50J1-142[»]
4GARX-ray3.30J1-142[»]
4GAUX-ray3.30J1-142[»]
4KIXX-ray2.90J1-142[»]
4KIZX-ray2.90J1-142[»]
4KJ1X-ray2.90J1-142[»]
4KJ3X-ray2.90J1-142[»]
4KJ5X-ray2.90J1-142[»]
4KJ7X-ray2.90J1-142[»]
4KJ9X-ray2.90J1-142[»]
4KJBX-ray2.90J1-142[»]
ProteinModelPortaliP0AA10.

Miscellaneous databases

EvolutionaryTraceiP0AA10.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0102.
HOGENOMiHOG000225286.
KOiK02871.
OMAiHQEFLKM.
OrthoDBiEOG628FBD.
PhylomeDBiP0AA10.

Family and domain databases

Gene3Di3.90.1180.10. 1 hit.
HAMAPiMF_01366. Ribosomal_L13.
InterProiIPR005822. Ribosomal_L13.
IPR005823. Ribosomal_L13_bac-type.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
[Graphical view]
PANTHERiPTHR11545. PTHR11545. 1 hit.
PfamiPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
PIRSFiPIRSF002181. Ribosomal_L13. 1 hit.
SUPFAMiSSF52161. SSF52161. 1 hit.
TIGRFAMsiTIGR01066. rplM_bact. 1 hit.
PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA10-1 [UniParc]FASTAAdd to Basket

« Hide

MKTFTAKPET VKRDWYVVDA TGKTLGRLAT ELARRLRGKH KAEYTPHVDT    50
GDYIIVLNAD KVAVTGNKRT DKVYYHHTGH IGGIKQATFE EMIARRPERV 100
IEIAVKGMLP KGPLGRAMFR KLKVYAGNEH NHAAQQPQVL DI 142
Length:142
Mass (Da):16,019
Last modified:July 21, 1986 - v1
Checksum:i58B45EF9EB75FDCD
GO

Mass spectrometryi

Molecular mass is 16018.0 Da from positions 1 - 142. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02130 Genomic DNA. Translation: CAA26041.1.
U18997 Genomic DNA. Translation: AAA58033.1.
U00096 Genomic DNA. Translation: AAC76263.1.
AP009048 Genomic DNA. Translation: BAE77274.1.
PIRiA02787. R5EC13.
RefSeqiNP_417698.1. NC_000913.3.
YP_491415.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76263; AAC76263; b3231.
BAE77274; BAE77274; BAE77274.
GeneIDi12932920.
947828.
KEGGiecj:Y75_p3151.
eco:b3231.
PATRICi32121888. VBIEscCol129921_3328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02130 Genomic DNA. Translation: CAA26041.1 .
U18997 Genomic DNA. Translation: AAA58033.1 .
U00096 Genomic DNA. Translation: AAC76263.1 .
AP009048 Genomic DNA. Translation: BAE77274.1 .
PIRi A02787. R5EC13.
RefSeqi NP_417698.1. NC_000913.3.
YP_491415.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 m 1-142 [» ]
1P85 electron microscopy 12.30 H 1-142 [» ]
1P86 electron microscopy 11.50 H 1-142 [» ]
1VS6 X-ray 3.46 J 1-142 [» ]
1VS8 X-ray 3.46 J 1-142 [» ]
1VT2 X-ray 3.30 J 1-142 [» ]
2AW4 X-ray 3.46 J 1-142 [» ]
2AWB X-ray 3.46 J 1-142 [» ]
2GYA electron microscopy 15.00 H 1-142 [» ]
2GYC electron microscopy 15.00 H 1-142 [» ]
2I2T X-ray 3.22 J 1-142 [» ]
2I2V X-ray 3.22 J 1-142 [» ]
2J28 electron microscopy 8.00 J 1-140 [» ]
2QAM X-ray 3.21 J 1-142 [» ]
2QAO X-ray 3.21 J 1-142 [» ]
2QBA X-ray 3.54 J 1-142 [» ]
2QBC X-ray 3.54 J 1-142 [» ]
2QBE X-ray 3.30 J 1-142 [» ]
2QBG X-ray 3.30 J 1-142 [» ]
2QBI X-ray 4.00 J 1-142 [» ]
2QBK X-ray 4.00 J 1-142 [» ]
2QOV X-ray 3.93 J 1-142 [» ]
2QOX X-ray 3.93 J 1-142 [» ]
2QOZ X-ray 3.50 J 1-142 [» ]
2QP1 X-ray 3.50 J 1-142 [» ]
2RDO electron microscopy 9.10 J 1-142 [» ]
2WWQ electron microscopy 5.80 J 1-142 [» ]
2Z4L X-ray 4.45 J 1-142 [» ]
2Z4N X-ray 4.45 J 1-142 [» ]
3BBX electron microscopy 10.00 J 1-142 [» ]
3E1B electron microscopy - 6 1-140 [» ]
3E1D electron microscopy - 6 1-140 [» ]
3FIK electron microscopy 6.70 J 1-142 [» ]
3I1N X-ray 3.19 J 1-142 [» ]
3I1P X-ray 3.19 J 1-142 [» ]
3I1R X-ray 3.81 J 1-142 [» ]
3I1T X-ray 3.81 J 1-142 [» ]
3I20 X-ray 3.71 J 1-142 [» ]
3I22 X-ray 3.71 J 1-142 [» ]
3IY9 electron microscopy 14.10 J 1-140 [» ]
3IZT electron microscopy - K 1-142 [» ]
3IZU electron microscopy - K 1-142 [» ]
3J01 electron microscopy - J 1-142 [» ]
3J0T electron microscopy 12.10 L 1-142 [» ]
3J0W electron microscopy 14.70 L 1-142 [» ]
3J0Y electron microscopy 13.50 L 1-142 [» ]
3J11 electron microscopy 13.10 L 1-142 [» ]
3J12 electron microscopy 11.50 L 1-142 [» ]
3J14 electron microscopy 11.50 L 1-142 [» ]
3J19 electron microscopy 8.30 J 1-142 [» ]
3J37 electron microscopy 9.80 N 1-142 [» ]
3J4X electron microscopy 12.00 J 1-142 [» ]
3J50 electron microscopy 20.00 J 1-142 [» ]
3J51 electron microscopy 17.00 J 1-142 [» ]
3J52 electron microscopy 12.00 J 1-142 [» ]
3J54 electron microscopy 13.00 J 1-142 [» ]
3J56 electron microscopy 15.00 J 1-142 [» ]
3J58 electron microscopy 17.00 J 1-142 [» ]
3J5A electron microscopy 12.00 J 1-142 [» ]
3J5C electron microscopy 17.00 J 1-142 [» ]
3J5E electron microscopy 17.00 J 1-142 [» ]
3J5G electron microscopy 20.00 J 1-142 [» ]
3J5I electron microscopy 15.00 J 1-142 [» ]
3J5K electron microscopy 9.00 J 1-142 [» ]
3J5L electron microscopy 6.60 J 1-142 [» ]
3J5O electron microscopy 6.80 J 1-142 [» ]
3J5U electron microscopy 7.60 L 1-142 [» ]
3J5W electron microscopy 7.60 M 1-142 [» ]
3KCR electron microscopy - J 1-142 [» ]
3OAS X-ray 3.25 J 1-142 [» ]
3OAT X-ray 3.25 J 1-142 [» ]
3OFC X-ray 3.19 J 1-142 [» ]
3OFD X-ray 3.19 J 1-142 [» ]
3OFQ X-ray 3.10 J 1-142 [» ]
3OFR X-ray 3.10 J 1-142 [» ]
3OFZ X-ray 3.29 J 1-142 [» ]
3OG0 X-ray 3.29 J 1-142 [» ]
3ORB X-ray 3.30 J 1-142 [» ]
3R8S X-ray 3.00 J 1-142 [» ]
3R8T X-ray 3.00 J 1-142 [» ]
3SGF X-ray 3.20 N 1-142 [» ]
3UOS X-ray 3.70 N 1-142 [» ]
4CSU electron microscopy 5.50 J 1-142 [» ]
4GAR X-ray 3.30 J 1-142 [» ]
4GAU X-ray 3.30 J 1-142 [» ]
4KIX X-ray 2.90 J 1-142 [» ]
4KIZ X-ray 2.90 J 1-142 [» ]
4KJ1 X-ray 2.90 J 1-142 [» ]
4KJ3 X-ray 2.90 J 1-142 [» ]
4KJ5 X-ray 2.90 J 1-142 [» ]
4KJ7 X-ray 2.90 J 1-142 [» ]
4KJ9 X-ray 2.90 J 1-142 [» ]
4KJB X-ray 2.90 J 1-142 [» ]
ProteinModelPortali P0AA10.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852140. 1 interaction.
DIPi DIP-47837N.
IntActi P0AA10. 112 interactions.
MINTi MINT-1269598.
STRINGi 511145.b3231.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0AA10.
PRIDEi P0AA10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76263 ; AAC76263 ; b3231 .
BAE77274 ; BAE77274 ; BAE77274 .
GeneIDi 12932920.
947828.
KEGGi ecj:Y75_p3151.
eco:b3231.
PATRICi 32121888. VBIEscCol129921_3328.

Organism-specific databases

EchoBASEi EB0867.
EcoGenei EG10874. rplM.

Phylogenomic databases

eggNOGi COG0102.
HOGENOMi HOG000225286.
KOi K02871.
OMAi HQEFLKM.
OrthoDBi EOG628FBD.
PhylomeDBi P0AA10.

Enzyme and pathway databases

BioCyci EcoCyc:EG10874-MONOMER.
ECOL316407:JW3200-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AA10.
PROi P0AA10.

Gene expression databases

Genevestigatori P0AA10.

Family and domain databases

Gene3Di 3.90.1180.10. 1 hit.
HAMAPi MF_01366. Ribosomal_L13.
InterProi IPR005822. Ribosomal_L13.
IPR005823. Ribosomal_L13_bac-type.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
[Graphical view ]
PANTHERi PTHR11545. PTHR11545. 1 hit.
Pfami PF00572. Ribosomal_L13. 1 hit.
[Graphical view ]
PIRSFi PIRSF002181. Ribosomal_L13. 1 hit.
SUPFAMi SSF52161. SSF52161. 1 hit.
TIGRFAMsi TIGR01066. rplM_bact. 1 hit.
PROSITEi PS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L13 from the large subunit of Escherichia coli ribosomes."
    Mende L.
    FEBS Lett. 96:313-316(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli."
    Isono S., Thamm S., Kitakawa M., Isono K.
    Mol. Gen. Genet. 198:279-282(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-46.
    Strain: K12 / EMG2.
  6. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  7. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  8. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL13_ECOLI
AccessioniPrimary (citable) accession number: P0AA10
Secondary accession number(s): P02410, Q2M8Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 90 of the entry and version 1 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

External Data

Dasty 3

Similar proteinsi