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Protein

50S ribosomal protein L32

Gene

rpmF

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10890-MONOMER.
ECOL316407:JW1075-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L32
Gene namesi
Name:rpmF
Ordered Locus Names:b1089, JW1075
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10890. rpmF.

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
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 575650S ribosomal protein L32PRO_0000172338Add
BLAST

Proteomic databases

PaxDbiP0A7N4.
PRIDEiP0A7N4.

Expressioni

Gene expression databases

GenevestigatoriP0A7N4.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L17 (PubMed:2665813).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
rpmBP0A7M22EBI-1112732,EBI-543024

Protein-protein interaction databases

DIPiDIP-35782N.
IntActiP0A7N4. 8 interactions.
STRINGi511145.b1089.

Structurei

Secondary structure

1
57
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167Combined sources
Helixi17 – 193Combined sources
Beta strandi28 – 303Combined sources
Turni32 – 343Combined sources
Beta strandi37 – 393Combined sources
Beta strandi40 – 423Combined sources
Beta strandi44 – 463Combined sources
Beta strandi47 – 493Combined sources
Beta strandi50 – 534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30Z2-57[»]
1P86electron microscopy11.50Z2-57[»]
1VS6X-ray3.4601-57[»]
1VS8X-ray3.4601-57[»]
1VT2X-ray3.3001-57[»]
2AW4X-ray3.4602-57[»]
2AWBX-ray3.4602-57[»]
2GYAelectron microscopy15.00Z28-56[»]
2GYCelectron microscopy15.00Z28-56[»]
2I2TX-ray3.2202-57[»]
2I2VX-ray3.2202-57[»]
2J28electron microscopy8.0002-57[»]
2QAMX-ray3.2102-57[»]
2QAOX-ray3.2102-57[»]
2QBAX-ray3.5402-57[»]
2QBCX-ray3.5402-57[»]
2QBEX-ray3.3002-57[»]
2QBGX-ray3.3002-57[»]
2QBIX-ray4.0002-57[»]
2QBKX-ray4.0002-57[»]
2QOVX-ray3.9302-57[»]
2QOXX-ray3.9302-57[»]
2QOZX-ray3.5002-57[»]
2QP1X-ray3.5002-57[»]
2RDOelectron microscopy9.1002-57[»]
2WWQelectron microscopy5.8032-57[»]
2Z4LX-ray4.4502-57[»]
2Z4NX-ray4.4502-57[»]
3BBXelectron microscopy10.0002-57[»]
3DF2X-ray3.5002-56[»]
3DF4X-ray3.5002-56[»]
3E1Belectron microscopy-T1-57[»]
3E1Delectron microscopy-T1-57[»]
3FIKelectron microscopy6.7002-57[»]
3I1NX-ray3.1901-57[»]
3I1PX-ray3.1901-57[»]
3I1RX-ray3.8101-57[»]
3I1TX-ray3.8101-57[»]
3I20X-ray3.7101-57[»]
3I22X-ray3.7101-57[»]
3IZTelectron microscopy-c1-57[»]
3IZUelectron microscopy-c1-57[»]
3J01electron microscopy-02-57[»]
3J0Telectron microscopy12.1032-57[»]
3J0Welectron microscopy14.7032-57[»]
3J0Yelectron microscopy13.5032-57[»]
3J11electron microscopy13.1032-57[»]
3J12electron microscopy11.5032-57[»]
3J14electron microscopy11.5032-57[»]
3J19electron microscopy8.3002-57[»]
3J37electron microscopy9.8052-57[»]
3J4Xelectron microscopy12.0001-57[»]
3J50electron microscopy20.0001-57[»]
3J51electron microscopy17.0001-57[»]
3J52electron microscopy12.0001-57[»]
3J54electron microscopy13.0001-57[»]
3J56electron microscopy15.0001-57[»]
3J58electron microscopy17.0001-57[»]
3J5Aelectron microscopy12.0001-57[»]
3J5Celectron microscopy17.0001-57[»]
3J5Eelectron microscopy17.0001-57[»]
3J5Gelectron microscopy20.0001-57[»]
3J5Ielectron microscopy15.0001-57[»]
3J5Kelectron microscopy9.0001-57[»]
3J5Lelectron microscopy6.6002-57[»]
3J5Oelectron microscopy6.8001-57[»]
3J5Uelectron microscopy7.6032-57[»]
3J5Welectron microscopy7.6042-57[»]
3J7Zelectron microscopy3.9001-57[»]
3KCRelectron microscopy-01-57[»]
3OASX-ray3.2502-57[»]
3OATX-ray3.2502-57[»]
3OFCX-ray3.1902-57[»]
3OFDX-ray3.1902-57[»]
3OFQX-ray3.1002-57[»]
3OFRX-ray3.1002-57[»]
3OFZX-ray3.2902-57[»]
3OG0X-ray3.2902-57[»]
3ORBX-ray3.3001-57[»]
3R8SX-ray3.0002-57[»]
3R8TX-ray3.0002-57[»]
3SGFX-ray3.2041-57[»]
3UOSX-ray3.7041-57[»]
4CSUelectron microscopy5.5032-57[»]
4GARX-ray3.3001-57[»]
4GAUX-ray3.3001-57[»]
4KIXX-ray2.9001-57[»]
4KIZX-ray2.9001-57[»]
4KJ1X-ray2.9001-57[»]
4KJ3X-ray2.9001-57[»]
4KJ5X-ray2.9001-57[»]
4KJ7X-ray2.9001-57[»]
4KJ9X-ray2.9001-57[»]
4KJBX-ray2.9001-57[»]
4PEBX-ray2.9502-57[»]
4PECX-ray2.9502-57[»]
4TOMX-ray3.0002-57[»]
4TOOX-ray3.0002-57[»]
4TOVX-ray2.9002-57[»]
4TOXX-ray2.9002-57[»]
4TP1X-ray2.9002-57[»]
4TP3X-ray2.9002-57[»]
4TP5X-ray2.9002-57[»]
4TP7X-ray2.9002-57[»]
4TP9X-ray2.8002-57[»]
4TPBX-ray2.8002-57[»]
4TPDX-ray2.8002-57[»]
4TPFX-ray2.8002-57[»]
4WAPX-ray3.0902-57[»]
4WARX-ray3.0902-57[»]
ProteinModelPortaliP0A7N4.
SMRiP0A7N4. Positions 2-57.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7N4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32P family.Curated

Phylogenomic databases

eggNOGiCOG0333.
HOGENOMiHOG000040269.
InParanoidiP0A7N4.
KOiK02911.
OMAiGEKHRRH.
OrthoDBiEOG6VMTT4.
PhylomeDBiP0A7N4.

Family and domain databases

HAMAPiMF_00340. Ribosomal_L32.
InterProiIPR002677. Ribosomal_L32p.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01783. Ribosomal_L32p. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01031. rpmF_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A7N4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVQQNKPTR SKRGMRRSHD ALTAVTSLSV DKTSGEKHLR HHITADGYYR

GRKVIAK
Length:57
Mass (Da):6,446
Last modified:January 23, 2007 - v2
Checksum:iFA07955DAA8E4E94
GO

Mass spectrometryi

Molecular mass is 6315.1 Da from positions 2 - 57. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29698 Genomic DNA. Translation: AAA24575.1.
U00096 Genomic DNA. Translation: AAC74173.1.
AP009048 Genomic DNA. Translation: BAA35897.1.
PIRiJV0048. R5EC32.
RefSeqiNP_415607.1. NC_000913.3.
YP_489357.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74173; AAC74173; b1089.
BAA35897; BAA35897; BAA35897.
GeneIDi12932035.
945657.
KEGGiecj:Y75_p1059.
eco:b1089.
PATRICi32117419. VBIEscCol129921_1132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29698 Genomic DNA. Translation: AAA24575.1.
U00096 Genomic DNA. Translation: AAC74173.1.
AP009048 Genomic DNA. Translation: BAA35897.1.
PIRiJV0048. R5EC32.
RefSeqiNP_415607.1. NC_000913.3.
YP_489357.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30Z2-57[»]
1P86electron microscopy11.50Z2-57[»]
1VS6X-ray3.4601-57[»]
1VS8X-ray3.4601-57[»]
1VT2X-ray3.3001-57[»]
2AW4X-ray3.4602-57[»]
2AWBX-ray3.4602-57[»]
2GYAelectron microscopy15.00Z28-56[»]
2GYCelectron microscopy15.00Z28-56[»]
2I2TX-ray3.2202-57[»]
2I2VX-ray3.2202-57[»]
2J28electron microscopy8.0002-57[»]
2QAMX-ray3.2102-57[»]
2QAOX-ray3.2102-57[»]
2QBAX-ray3.5402-57[»]
2QBCX-ray3.5402-57[»]
2QBEX-ray3.3002-57[»]
2QBGX-ray3.3002-57[»]
2QBIX-ray4.0002-57[»]
2QBKX-ray4.0002-57[»]
2QOVX-ray3.9302-57[»]
2QOXX-ray3.9302-57[»]
2QOZX-ray3.5002-57[»]
2QP1X-ray3.5002-57[»]
2RDOelectron microscopy9.1002-57[»]
2WWQelectron microscopy5.8032-57[»]
2Z4LX-ray4.4502-57[»]
2Z4NX-ray4.4502-57[»]
3BBXelectron microscopy10.0002-57[»]
3DF2X-ray3.5002-56[»]
3DF4X-ray3.5002-56[»]
3E1Belectron microscopy-T1-57[»]
3E1Delectron microscopy-T1-57[»]
3FIKelectron microscopy6.7002-57[»]
3I1NX-ray3.1901-57[»]
3I1PX-ray3.1901-57[»]
3I1RX-ray3.8101-57[»]
3I1TX-ray3.8101-57[»]
3I20X-ray3.7101-57[»]
3I22X-ray3.7101-57[»]
3IZTelectron microscopy-c1-57[»]
3IZUelectron microscopy-c1-57[»]
3J01electron microscopy-02-57[»]
3J0Telectron microscopy12.1032-57[»]
3J0Welectron microscopy14.7032-57[»]
3J0Yelectron microscopy13.5032-57[»]
3J11electron microscopy13.1032-57[»]
3J12electron microscopy11.5032-57[»]
3J14electron microscopy11.5032-57[»]
3J19electron microscopy8.3002-57[»]
3J37electron microscopy9.8052-57[»]
3J4Xelectron microscopy12.0001-57[»]
3J50electron microscopy20.0001-57[»]
3J51electron microscopy17.0001-57[»]
3J52electron microscopy12.0001-57[»]
3J54electron microscopy13.0001-57[»]
3J56electron microscopy15.0001-57[»]
3J58electron microscopy17.0001-57[»]
3J5Aelectron microscopy12.0001-57[»]
3J5Celectron microscopy17.0001-57[»]
3J5Eelectron microscopy17.0001-57[»]
3J5Gelectron microscopy20.0001-57[»]
3J5Ielectron microscopy15.0001-57[»]
3J5Kelectron microscopy9.0001-57[»]
3J5Lelectron microscopy6.6002-57[»]
3J5Oelectron microscopy6.8001-57[»]
3J5Uelectron microscopy7.6032-57[»]
3J5Welectron microscopy7.6042-57[»]
3J7Zelectron microscopy3.9001-57[»]
3KCRelectron microscopy-01-57[»]
3OASX-ray3.2502-57[»]
3OATX-ray3.2502-57[»]
3OFCX-ray3.1902-57[»]
3OFDX-ray3.1902-57[»]
3OFQX-ray3.1002-57[»]
3OFRX-ray3.1002-57[»]
3OFZX-ray3.2902-57[»]
3OG0X-ray3.2902-57[»]
3ORBX-ray3.3001-57[»]
3R8SX-ray3.0002-57[»]
3R8TX-ray3.0002-57[»]
3SGFX-ray3.2041-57[»]
3UOSX-ray3.7041-57[»]
4CSUelectron microscopy5.5032-57[»]
4GARX-ray3.3001-57[»]
4GAUX-ray3.3001-57[»]
4KIXX-ray2.9001-57[»]
4KIZX-ray2.9001-57[»]
4KJ1X-ray2.9001-57[»]
4KJ3X-ray2.9001-57[»]
4KJ5X-ray2.9001-57[»]
4KJ7X-ray2.9001-57[»]
4KJ9X-ray2.9001-57[»]
4KJBX-ray2.9001-57[»]
4PEBX-ray2.9502-57[»]
4PECX-ray2.9502-57[»]
4TOMX-ray3.0002-57[»]
4TOOX-ray3.0002-57[»]
4TOVX-ray2.9002-57[»]
4TOXX-ray2.9002-57[»]
4TP1X-ray2.9002-57[»]
4TP3X-ray2.9002-57[»]
4TP5X-ray2.9002-57[»]
4TP7X-ray2.9002-57[»]
4TP9X-ray2.8002-57[»]
4TPBX-ray2.8002-57[»]
4TPDX-ray2.8002-57[»]
4TPFX-ray2.8002-57[»]
4WAPX-ray3.0902-57[»]
4WARX-ray3.0902-57[»]
ProteinModelPortaliP0A7N4.
SMRiP0A7N4. Positions 2-57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35782N.
IntActiP0A7N4. 8 interactions.
STRINGi511145.b1089.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7N4.
PRIDEiP0A7N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74173; AAC74173; b1089.
BAA35897; BAA35897; BAA35897.
GeneIDi12932035.
945657.
KEGGiecj:Y75_p1059.
eco:b1089.
PATRICi32117419. VBIEscCol129921_1132.

Organism-specific databases

EchoBASEiEB0883.
EcoGeneiEG10890. rpmF.

Phylogenomic databases

eggNOGiCOG0333.
HOGENOMiHOG000040269.
InParanoidiP0A7N4.
KOiK02911.
OMAiGEKHRRH.
OrthoDBiEOG6VMTT4.
PhylomeDBiP0A7N4.

Enzyme and pathway databases

BioCyciEcoCyc:EG10890-MONOMER.
ECOL316407:JW1075-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7N4.
PROiP0A7N4.

Gene expression databases

GenevestigatoriP0A7N4.

Family and domain databases

HAMAPiMF_00340. Ribosomal_L32.
InterProiIPR002677. Ribosomal_L32p.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PfamiPF01783. Ribosomal_L32p. 1 hit.
[Graphical view]
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR01031. rpmF_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and analysis of an Escherichia coli operon containing the rpmF gene for ribosomal protein L32 and the gene for a 30-kilodalton protein."
    Tanaka Y., Tsujimura A., Fujita N., Isono S., Isono K.
    J. Bacteriol. 171:5707-5712(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "The primary structure of protein L32 from the 50S subunit of Escherichia coli ribosomes."
    Wittmann-Liebold B., Greuer B., Pannenbecker R.
    Hoppe-Seyler's Z. Physiol. Chem. 356:1977-1979(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-57.
    Strain: K.
  6. "The primary structure of ribosomal protein L32 from E. coli MRE-600 ribosomes."
    Vinokurov L.M., Alakhov Y.B., Golov E.A., Ovchinnikov Y.A.
    Bioorg. Khim. 2:1013-1017(1976)
    Cited for: PROTEIN SEQUENCE OF 2-57.
    Strain: MRE-600.
  7. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
    Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
    Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L17.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "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.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL32_ECOLI
AccessioniPrimary (citable) accession number: P0A7N4
Secondary accession number(s): P02435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 94 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

External Data

Dasty 3

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 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.