Skip Header

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

Q5SHP3

- RL22_THET8

UniProt

Q5SHP3 - RL22_THET8

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

50S ribosomal protein L22

Gene

rplV

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

Functioni

This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).By similarity
The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome. This extension seems to form part of the wall of the exit tunnel.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1726-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L22
Gene namesi
Name:rplV
Ordered Locus Names:TTHA1687
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
Chaini1 – 11311350S ribosomal protein L22PRO_0000125249Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA1687.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Helixi14 – 2411Combined sources
Beta strandi25 – 284Combined sources
Helixi29 – 379Combined sources
Helixi43 – 6220Combined sources
Helixi66 – 683Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi82 – 876Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 986Combined sources
Beta strandi101 – 1099Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50S1-113[»]
1ML5electron microscopy14.00s1-113[»]
1VVMX-ray3.22W1-113[»]
1VVOX-ray3.22W1-113[»]
1VVQX-ray3.90W1-113[»]
1VVSX-ray3.90W1-113[»]
1VVUX-ray3.90W1-113[»]
1VVWX-ray3.90W1-113[»]
1VVYX-ray3.92W1-113[»]
1VW0X-ray3.92W1-113[»]
1VX9X-ray2.94W1-113[»]
1VXJX-ray2.94W1-113[»]
1VXLX-ray3.48W1-113[»]
1VXNX-ray3.48W1-113[»]
1VXQX-ray3.14W1-113[»]
1VXTX-ray3.14W1-113[»]
1VY1X-ray3.68W1-113[»]
1VY3X-ray3.68W1-113[»]
1YL3X-ray5.50S1-113[»]
2B66X-ray5.90W1-113[»]
2B9NX-ray6.76W1-113[»]
2B9PX-ray6.46W1-113[»]
2HGJX-ray5.00V1-113[»]
2HGQX-ray5.50V1-113[»]
2HGUX-ray4.51V1-113[»]
2J01X-ray2.80W1-113[»]
2J03X-ray2.80W1-113[»]
2V47X-ray3.80W1-113[»]
2V49X-ray3.80W1-113[»]
2WDIX-ray3.30W1-113[»]
2WDJX-ray3.30W1-113[»]
2WDLX-ray3.50W1-113[»]
2WDNX-ray3.50W1-113[»]
2WH2X-ray3.45W1-113[»]
2WH4X-ray3.45W1-113[»]
2WRJX-ray3.60W1-113[»]
2WRLX-ray3.60W1-113[»]
2WROX-ray3.60W1-113[»]
2WRRX-ray3.60W1-113[»]
2X9SX-ray3.10W1-113[»]
2X9UX-ray3.10W1-113[»]
2XG0X-ray3.20W1-113[»]
2XG2X-ray3.20W1-113[»]
2XQEX-ray3.10W1-113[»]
2XTGelectron microscopy7.80W1-113[»]
2XUXelectron microscopy7.60W1-113[»]
2Y0VX-ray3.10W1-113[»]
2Y0XX-ray3.10W1-113[»]
2Y0ZX-ray3.10W1-113[»]
2Y11X-ray3.10W1-113[»]
2Y13X-ray3.10W1-113[»]
2Y15X-ray3.10W1-113[»]
2Y17X-ray3.10W1-113[»]
2Y19X-ray3.10W1-113[»]
3FINelectron microscopy6.40W1-113[»]
3HUXX-ray3.10W1-113[»]
3HUZX-ray3.10W1-113[»]
3I8FX-ray3.10S1-113[»]
3I8IX-ray3.10S1-113[»]
3I9CX-ray3.50S1-113[»]
3I9EX-ray3.50S1-113[»]
3KIRX-ray3.30W1-113[»]
3KITX-ray3.30W1-113[»]
3KIWX-ray3.60W1-113[»]
3KIYX-ray3.60W1-113[»]
3KNIX-ray3.00W1-113[»]
3KNKX-ray3.00W1-113[»]
3KNMX-ray3.45W1-113[»]
3KNOX-ray3.45W1-113[»]
3TVEX-ray3.10S1-113[»]
3TVHX-ray3.10S1-113[»]
3UXQX-ray3.20W1-113[»]
3UXRX-ray3.20W1-113[»]
3UYEX-ray3.00S1-113[»]
3UYGX-ray3.00S1-113[»]
3UZ1X-ray3.30S1-113[»]
3UZ2X-ray3.30S1-113[»]
3UZ8X-ray3.00S1-113[»]
3UZ9X-ray3.00S1-113[»]
3UZFX-ray3.30S1-113[»]
3UZHX-ray3.30S1-113[»]
3UZKX-ray3.30S1-113[»]
3UZNX-ray3.30S1-113[»]
3V23X-ray3.00W1-113[»]
3V25X-ray3.00W1-113[»]
3V27X-ray3.10W1-113[»]
3V29X-ray3.10W1-113[»]
3V2DX-ray2.70W1-113[»]
3V2FX-ray2.70W1-113[»]
3V6WX-ray3.90W1-113[»]
3V6XX-ray3.90W1-113[»]
3ZN9X-ray3.10W1-113[»]
3ZNEX-ray3.10W1-113[»]
3ZVPX-ray3.80W1-113[»]
4ABSX-ray3.10W1-113[»]
4B8GX-ray3.70W1-113[»]
4B8IX-ray3.70W1-113[»]
4BTDX-ray2.95W1-113[»]
4BYCX-ray3.35W1-113[»]
4BYEX-ray3.35W1-113[»]
4DHAX-ray3.20W1-113[»]
4DHCX-ray3.20W1-113[»]
4EJBX-ray3.52W1-113[»]
4EJCX-ray3.52W1-113[»]
4G5LX-ray3.30S1-113[»]
4G5NX-ray3.30S1-113[»]
4G5UX-ray3.10S1-113[»]
4G5WX-ray3.10S1-113[»]
4JUXX-ray2.86W1-113[»]
4K0MX-ray3.30W1-112[»]
4K0QX-ray3.30W1-112[»]
4KX0X-ray3.44W1-113[»]
4KX2X-ray3.44W1-113[»]
4NVVX-ray3.00W1-113[»]
4NVXX-ray3.00W1-113[»]
4NVZX-ray3.10W1-113[»]
4NW1X-ray3.10W1-113[»]
4QCNX-ray2.60W1-113[»]
4QCPX-ray2.60W1-113[»]
4QCRX-ray2.55W1-113[»]
4QCTX-ray2.55W1-113[»]
4QCVX-ray2.90W1-113[»]
4QCXX-ray2.90W1-113[»]
4QCZX-ray2.80W1-113[»]
4QD1X-ray2.80W1-113[»]
4QJSX-ray2.90W1-113[»]
4W2BX-ray3.60R1-113[»]
4W2DX-ray3.60R1-113[»]
ProteinModelPortaliQ5SHP3.
SMRiQ5SHP3. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHP3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Phylogenomic databases

eggNOGiCOG0091.
HOGENOMiHOG000205046.
KOiK02890.
OMAiMKRIRPR.
OrthoDBiEOG6V4GKB.
PhylomeDBiQ5SHP3.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_B. Ribosomal_L22_B.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view]
PANTHERiPTHR13501. PTHR13501. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01044. rplV_bact. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHP3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAKAIARYV RISPRKVRLV VDLIRGKSLE EARNILRYTN KRGAYFVAKV
60 70 80 90 100
LESAAANAVN NHDMLEDRLY VKAAYVDEGP ALKRVLPRAR GRADIIKKRT
110
SHITVILGEK HGK
Length:113
Mass (Da):12,780
Last modified:December 21, 2004 - v1
Checksum:i11814D2DE644AF1F
GO

Mass spectrometryi

Molecular mass is 12781 Da from positions 1 - 113. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71510.1.
RefSeqiWP_011173710.1. NC_006461.1.
YP_144953.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71510; BAD71510; BAD71510.
GeneIDi3169835.
KEGGittj:TTHA1687.
PATRICi23958329. VBITheThe93045_1657.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71510.1 .
RefSeqi WP_011173710.1. NC_006461.1.
YP_144953.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GIY X-ray 5.50 S 1-113 [» ]
1ML5 electron microscopy 14.00 s 1-113 [» ]
1VVM X-ray 3.22 W 1-113 [» ]
1VVO X-ray 3.22 W 1-113 [» ]
1VVQ X-ray 3.90 W 1-113 [» ]
1VVS X-ray 3.90 W 1-113 [» ]
1VVU X-ray 3.90 W 1-113 [» ]
1VVW X-ray 3.90 W 1-113 [» ]
1VVY X-ray 3.92 W 1-113 [» ]
1VW0 X-ray 3.92 W 1-113 [» ]
1VX9 X-ray 2.94 W 1-113 [» ]
1VXJ X-ray 2.94 W 1-113 [» ]
1VXL X-ray 3.48 W 1-113 [» ]
1VXN X-ray 3.48 W 1-113 [» ]
1VXQ X-ray 3.14 W 1-113 [» ]
1VXT X-ray 3.14 W 1-113 [» ]
1VY1 X-ray 3.68 W 1-113 [» ]
1VY3 X-ray 3.68 W 1-113 [» ]
1YL3 X-ray 5.50 S 1-113 [» ]
2B66 X-ray 5.90 W 1-113 [» ]
2B9N X-ray 6.76 W 1-113 [» ]
2B9P X-ray 6.46 W 1-113 [» ]
2HGJ X-ray 5.00 V 1-113 [» ]
2HGQ X-ray 5.50 V 1-113 [» ]
2HGU X-ray 4.51 V 1-113 [» ]
2J01 X-ray 2.80 W 1-113 [» ]
2J03 X-ray 2.80 W 1-113 [» ]
2V47 X-ray 3.80 W 1-113 [» ]
2V49 X-ray 3.80 W 1-113 [» ]
2WDI X-ray 3.30 W 1-113 [» ]
2WDJ X-ray 3.30 W 1-113 [» ]
2WDL X-ray 3.50 W 1-113 [» ]
2WDN X-ray 3.50 W 1-113 [» ]
2WH2 X-ray 3.45 W 1-113 [» ]
2WH4 X-ray 3.45 W 1-113 [» ]
2WRJ X-ray 3.60 W 1-113 [» ]
2WRL X-ray 3.60 W 1-113 [» ]
2WRO X-ray 3.60 W 1-113 [» ]
2WRR X-ray 3.60 W 1-113 [» ]
2X9S X-ray 3.10 W 1-113 [» ]
2X9U X-ray 3.10 W 1-113 [» ]
2XG0 X-ray 3.20 W 1-113 [» ]
2XG2 X-ray 3.20 W 1-113 [» ]
2XQE X-ray 3.10 W 1-113 [» ]
2XTG electron microscopy 7.80 W 1-113 [» ]
2XUX electron microscopy 7.60 W 1-113 [» ]
2Y0V X-ray 3.10 W 1-113 [» ]
2Y0X X-ray 3.10 W 1-113 [» ]
2Y0Z X-ray 3.10 W 1-113 [» ]
2Y11 X-ray 3.10 W 1-113 [» ]
2Y13 X-ray 3.10 W 1-113 [» ]
2Y15 X-ray 3.10 W 1-113 [» ]
2Y17 X-ray 3.10 W 1-113 [» ]
2Y19 X-ray 3.10 W 1-113 [» ]
3FIN electron microscopy 6.40 W 1-113 [» ]
3HUX X-ray 3.10 W 1-113 [» ]
3HUZ X-ray 3.10 W 1-113 [» ]
3I8F X-ray 3.10 S 1-113 [» ]
3I8I X-ray 3.10 S 1-113 [» ]
3I9C X-ray 3.50 S 1-113 [» ]
3I9E X-ray 3.50 S 1-113 [» ]
3KIR X-ray 3.30 W 1-113 [» ]
3KIT X-ray 3.30 W 1-113 [» ]
3KIW X-ray 3.60 W 1-113 [» ]
3KIY X-ray 3.60 W 1-113 [» ]
3KNI X-ray 3.00 W 1-113 [» ]
3KNK X-ray 3.00 W 1-113 [» ]
3KNM X-ray 3.45 W 1-113 [» ]
3KNO X-ray 3.45 W 1-113 [» ]
3TVE X-ray 3.10 S 1-113 [» ]
3TVH X-ray 3.10 S 1-113 [» ]
3UXQ X-ray 3.20 W 1-113 [» ]
3UXR X-ray 3.20 W 1-113 [» ]
3UYE X-ray 3.00 S 1-113 [» ]
3UYG X-ray 3.00 S 1-113 [» ]
3UZ1 X-ray 3.30 S 1-113 [» ]
3UZ2 X-ray 3.30 S 1-113 [» ]
3UZ8 X-ray 3.00 S 1-113 [» ]
3UZ9 X-ray 3.00 S 1-113 [» ]
3UZF X-ray 3.30 S 1-113 [» ]
3UZH X-ray 3.30 S 1-113 [» ]
3UZK X-ray 3.30 S 1-113 [» ]
3UZN X-ray 3.30 S 1-113 [» ]
3V23 X-ray 3.00 W 1-113 [» ]
3V25 X-ray 3.00 W 1-113 [» ]
3V27 X-ray 3.10 W 1-113 [» ]
3V29 X-ray 3.10 W 1-113 [» ]
3V2D X-ray 2.70 W 1-113 [» ]
3V2F X-ray 2.70 W 1-113 [» ]
3V6W X-ray 3.90 W 1-113 [» ]
3V6X X-ray 3.90 W 1-113 [» ]
3ZN9 X-ray 3.10 W 1-113 [» ]
3ZNE X-ray 3.10 W 1-113 [» ]
3ZVP X-ray 3.80 W 1-113 [» ]
4ABS X-ray 3.10 W 1-113 [» ]
4B8G X-ray 3.70 W 1-113 [» ]
4B8I X-ray 3.70 W 1-113 [» ]
4BTD X-ray 2.95 W 1-113 [» ]
4BYC X-ray 3.35 W 1-113 [» ]
4BYE X-ray 3.35 W 1-113 [» ]
4DHA X-ray 3.20 W 1-113 [» ]
4DHC X-ray 3.20 W 1-113 [» ]
4EJB X-ray 3.52 W 1-113 [» ]
4EJC X-ray 3.52 W 1-113 [» ]
4G5L X-ray 3.30 S 1-113 [» ]
4G5N X-ray 3.30 S 1-113 [» ]
4G5U X-ray 3.10 S 1-113 [» ]
4G5W X-ray 3.10 S 1-113 [» ]
4JUX X-ray 2.86 W 1-113 [» ]
4K0M X-ray 3.30 W 1-112 [» ]
4K0Q X-ray 3.30 W 1-112 [» ]
4KX0 X-ray 3.44 W 1-113 [» ]
4KX2 X-ray 3.44 W 1-113 [» ]
4NVV X-ray 3.00 W 1-113 [» ]
4NVX X-ray 3.00 W 1-113 [» ]
4NVZ X-ray 3.10 W 1-113 [» ]
4NW1 X-ray 3.10 W 1-113 [» ]
4QCN X-ray 2.60 W 1-113 [» ]
4QCP X-ray 2.60 W 1-113 [» ]
4QCR X-ray 2.55 W 1-113 [» ]
4QCT X-ray 2.55 W 1-113 [» ]
4QCV X-ray 2.90 W 1-113 [» ]
4QCX X-ray 2.90 W 1-113 [» ]
4QCZ X-ray 2.80 W 1-113 [» ]
4QD1 X-ray 2.80 W 1-113 [» ]
4QJS X-ray 2.90 W 1-113 [» ]
4W2B X-ray 3.60 R 1-113 [» ]
4W2D X-ray 3.60 R 1-113 [» ]
ProteinModelPortali Q5SHP3.
SMRi Q5SHP3. Positions 1-113.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71510 ; BAD71510 ; BAD71510 .
GeneIDi 3169835.
KEGGi ttj:TTHA1687.
PATRICi 23958329. VBITheThe93045_1657.

Phylogenomic databases

eggNOGi COG0091.
HOGENOMi HOG000205046.
KOi K02890.
OMAi MKRIRPR.
OrthoDBi EOG6V4GKB.
PhylomeDBi Q5SHP3.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1726-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SHP3.

Family and domain databases

Gene3Di 3.90.470.10. 1 hit.
HAMAPi MF_01331_B. Ribosomal_L22_B.
InterProi IPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005727. Ribosomal_L22_bac/chlpt-type.
[Graphical view ]
PANTHERi PTHR13501. PTHR13501. 1 hit.
Pfami PF00237. Ribosomal_L22. 1 hit.
[Graphical view ]
SUPFAMi SSF54843. SSF54843. 1 hit.
TIGRFAMsi TIGR01044. rplV_bact. 1 hit.
PROSITEi PS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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 1-20.
  3. "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.
  4. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL22_THET8
AccessioniPrimary (citable) accession number: Q5SHP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: November 26, 2014
This is version 83 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. 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