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Protein

50S ribosomal protein L32

Gene

rpmF

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Found on the solvent side of the large subunit.

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

BioCyciTTHE300852:GH8R-439-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L32
Gene namesi
Name:rpmF
Synonyms:rpl32
Ordered Locus Names:TTHA0418
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 605950S ribosomal protein L32PRO_0000172427Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA0418.

Structurei

Secondary structure

1
60
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 197Combined sources
Helixi20 – 223Combined sources
Beta strandi31 – 333Combined sources
Turni34 – 363Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 443Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 543Combined sources
Beta strandi55 – 573Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.4451-60[»]
1VY4X-ray2.6051-60[»]
1VY5X-ray2.5551-60[»]
1VY6X-ray2.9051-60[»]
1VY7X-ray2.8051-60[»]
4L47X-ray3.2251-60[»]
4L71X-ray3.9051-60[»]
4LELX-ray3.9051-60[»]
4LFZX-ray3.9251-60[»]
4LNTX-ray2.9451-60[»]
4LSKX-ray3.4851-60[»]
4LT8X-ray3.1451-60[»]
4P6FX-ray3.60a1-60[»]
4P70X-ray3.6851-60[»]
4V4PX-ray5.5051-60[»]
4V4XX-ray5.0041-60[»]
4V4YX-ray5.5041-60[»]
4V4ZX-ray4.5141-60[»]
4V51X-ray2.8052-60[»]
4V5AX-ray3.5052-60[»]
4V5CX-ray3.3051-60[»]
4V5DX-ray3.5051-60[»]
4V5EX-ray3.4551-60[»]
4V5FX-ray3.6051-60[»]
4V5GX-ray3.6051-60[»]
4V5JX-ray3.1051-60[»]
4V5KX-ray3.2051-60[»]
4V5LX-ray3.1051-60[»]
4V5Melectron microscopy7.8051-60[»]
4V5Nelectron microscopy7.6051-60[»]
4V5PX-ray3.1051-60[»]
4V5QX-ray3.1051-60[»]
4V5RX-ray3.1051-60[»]
4V5SX-ray3.1051-60[»]
4V68electron microscopy6.4052-60[»]
4V6AX-ray3.1051-60[»]
4V6FX-ray3.1051-60[»]
4V6GX-ray3.5051-60[»]
4V7JX-ray3.3051-60[»]
4V7KX-ray3.6051-60[»]
4V7LX-ray3.0051-60[»]
4V7MX-ray3.4551-60[»]
4V7WX-ray3.0051-60[»]
4V7XX-ray3.0051-60[»]
4V7YX-ray3.0051-60[»]
4V7ZX-ray3.1051-60[»]
4V87X-ray3.1052-60[»]
4V8AX-ray3.2051-60[»]
4V8BX-ray3.0051-60[»]
4V8CX-ray3.3051-60[»]
4V8DX-ray3.0051-60[»]
4V8EX-ray3.3051-60[»]
4V8FX-ray3.3051-60[»]
4V8GX-ray3.0051-60[»]
4V8HX-ray3.1051-60[»]
4V8IX-ray2.7051-60[»]
4V8JX-ray3.9051-60[»]
4V8NX-ray3.1051-60[»]
4V8OX-ray3.8051-60[»]
4V8QX-ray3.1051-60[»]
4V8UX-ray3.7051-60[»]
4V8XX-ray3.3551-60[»]
4V90X-ray2.9552-60[»]
4V95X-ray3.2051-60[»]
4V97X-ray3.5251-60[»]
4V9AX-ray3.3051-60[»]
4V9BX-ray3.1051-60[»]
4V9HX-ray2.8651-60[»]
4V9IX-ray3.3052-60[»]
4V9RX-ray3.0051-60[»]
4V9SX-ray3.1051-60[»]
4W2EX-ray2.9051-60[»]
4W2FX-ray2.4051-60[»]
4W2GX-ray2.5551-60[»]
4W2HX-ray2.7051-60[»]
4W2IX-ray2.7051-60[»]
ProteinModelPortaliP80339.
SMRiP80339. Positions 2-60.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80339.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32P family.Curated

Phylogenomic databases

eggNOGiCOG0333.
HOGENOMiHOG000040268.
KOiK02911.
OMAiRTHFKLA.
OrthoDBiEOG6VMTT4.
PhylomeDBiP80339.

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.

P80339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKHPVPKKK TSKARRDARR SHHALTPPTL VPCPECKAMK PPHTVCPECG
60
YYAGRKVLEV
Length:60
Mass (Da):6,705
Last modified:January 23, 2007 - v5
Checksum:i3B972CB90FF2DE59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171D → A AA sequence (PubMed:11154066).Curated
Sequence conflicti32 – 332PC → VP AA sequence (Ref. 2) Curated
Sequence conflicti36 – 361C → I AA sequence (Ref. 2) Curated
Sequence conflicti41 – 411P → H AA sequence (Ref. 2) Curated

Mass spectrometryi

Molecular mass is 6575 Da from positions 2 - 60. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70241.1.
RefSeqiYP_143684.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70241; BAD70241; BAD70241.
GeneIDi3168304.
KEGGittj:TTHA0418.
PATRICi23955807. VBITheThe93045_0418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70241.1.
RefSeqiYP_143684.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.4451-60[»]
1VY4X-ray2.6051-60[»]
1VY5X-ray2.5551-60[»]
1VY6X-ray2.9051-60[»]
1VY7X-ray2.8051-60[»]
4L47X-ray3.2251-60[»]
4L71X-ray3.9051-60[»]
4LELX-ray3.9051-60[»]
4LFZX-ray3.9251-60[»]
4LNTX-ray2.9451-60[»]
4LSKX-ray3.4851-60[»]
4LT8X-ray3.1451-60[»]
4P6FX-ray3.60a1-60[»]
4P70X-ray3.6851-60[»]
4V4PX-ray5.5051-60[»]
4V4XX-ray5.0041-60[»]
4V4YX-ray5.5041-60[»]
4V4ZX-ray4.5141-60[»]
4V51X-ray2.8052-60[»]
4V5AX-ray3.5052-60[»]
4V5CX-ray3.3051-60[»]
4V5DX-ray3.5051-60[»]
4V5EX-ray3.4551-60[»]
4V5FX-ray3.6051-60[»]
4V5GX-ray3.6051-60[»]
4V5JX-ray3.1051-60[»]
4V5KX-ray3.2051-60[»]
4V5LX-ray3.1051-60[»]
4V5Melectron microscopy7.8051-60[»]
4V5Nelectron microscopy7.6051-60[»]
4V5PX-ray3.1051-60[»]
4V5QX-ray3.1051-60[»]
4V5RX-ray3.1051-60[»]
4V5SX-ray3.1051-60[»]
4V68electron microscopy6.4052-60[»]
4V6AX-ray3.1051-60[»]
4V6FX-ray3.1051-60[»]
4V6GX-ray3.5051-60[»]
4V7JX-ray3.3051-60[»]
4V7KX-ray3.6051-60[»]
4V7LX-ray3.0051-60[»]
4V7MX-ray3.4551-60[»]
4V7WX-ray3.0051-60[»]
4V7XX-ray3.0051-60[»]
4V7YX-ray3.0051-60[»]
4V7ZX-ray3.1051-60[»]
4V87X-ray3.1052-60[»]
4V8AX-ray3.2051-60[»]
4V8BX-ray3.0051-60[»]
4V8CX-ray3.3051-60[»]
4V8DX-ray3.0051-60[»]
4V8EX-ray3.3051-60[»]
4V8FX-ray3.3051-60[»]
4V8GX-ray3.0051-60[»]
4V8HX-ray3.1051-60[»]
4V8IX-ray2.7051-60[»]
4V8JX-ray3.9051-60[»]
4V8NX-ray3.1051-60[»]
4V8OX-ray3.8051-60[»]
4V8QX-ray3.1051-60[»]
4V8UX-ray3.7051-60[»]
4V8XX-ray3.3551-60[»]
4V90X-ray2.9552-60[»]
4V95X-ray3.2051-60[»]
4V97X-ray3.5251-60[»]
4V9AX-ray3.3051-60[»]
4V9BX-ray3.1051-60[»]
4V9HX-ray2.8651-60[»]
4V9IX-ray3.3052-60[»]
4V9RX-ray3.0051-60[»]
4V9SX-ray3.1051-60[»]
4W2EX-ray2.9051-60[»]
4W2FX-ray2.4051-60[»]
4W2GX-ray2.5551-60[»]
4W2HX-ray2.7051-60[»]
4W2IX-ray2.7051-60[»]
ProteinModelPortaliP80339.
SMRiP80339. Positions 2-60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70241; BAD70241; BAD70241.
GeneIDi3168304.
KEGGittj:TTHA0418.
PATRICi23955807. VBITheThe93045_0418.

Phylogenomic databases

eggNOGiCOG0333.
HOGENOMiHOG000040268.
KOiK02911.
OMAiRTHFKLA.
OrthoDBiEOG6VMTT4.
PhylomeDBiP80339.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-439-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP80339.

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. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "The isolation and complete amino acid sequence of the ribosomal protein L36 from Thermus thermophilus and its zinc-binding motif."
    Boysen R.I., Lorenz S., Kim J.S., Schroeder W.F.K.J., Erdmann V.A.
    Endocyt. Cell Res. 11:41-58(1995)
    Cited for: PROTEIN SEQUENCE OF 2-41.
  3. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17.
  4. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  5. Cited for: STRUCTURE OF THE RIBOSOME.

Entry informationi

Entry nameiRL32_THET8
AccessioniPrimary (citable) accession number: P80339
Secondary accession number(s): O05480, Q5SL75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 115 of the entry and version 5 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.