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Protein

30S ribosomal protein S12

Gene

rpsL

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

Functioni

With S4 and S5 plays an important role in translational accuracy.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).By similarity1 Publication
Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit.1 Publication

Miscellaneous

At least 19 substitutions or deletions in 11 codons can promote streptomycin resistance, dependence or pseudodependence; all but one of the streptomycin resistant mutations (K42R) are associated with hyperaccurate translation and thus reduced translational efficiency.2 Publications
The streptomycin sensitive allele is dominant to resistant alleles.

GO - Molecular functioni

  • misfolded RNA binding Source: EcoCyc
  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • Group I intron splicing Source: EcoCyc
  • maintenance of translational fidelity Source: EcoCyc
  • positive regulation of RNA splicing Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
  • RNA folding Source: EcoCyc
  • translation Source: EcoCyc

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10911-MONOMER.
MetaCyc:EG10911-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S12
Alternative name(s):
Small ribosomal subunit protein uS121 Publication
Gene namesi
Name:rpsL
Synonyms:strA
Ordered Locus Names:b3342, JW3304
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10911. rpsL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoliWiki

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi57L → H: Protein is not incorporated into ribosomes. 1 Publication1
Mutagenesisi88K → Q: Confers low-level resistance to streptomycin and a 15% decrease in the translational elongation rate. 1 Publication1

Chemistry databases

DrugBankiDB00479. Amikacin.
DB06696. Arbekacin.
DB00452. Framycetin.
DB00798. Gentamicin.
DB04729. GENTAMICIN C1A.
DB01172. Kanamycin.
DB00994. Neomycin.
DB00955. Netilmicin.
DB03615. Ribostamycin.
DB00919. Spectinomycin.
DB01082. Streptomycin.
DB00560. Tigecycline.
DB00684. Tobramycin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001462192 – 12430S ribosomal protein S12Add BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei893-methylthioaspartic acid1 Publication1
Modified residuei108N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP0A7S3.
PRIDEiP0A7S3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:320034, PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12093756, PubMed:12379845, PubMed:12244297, PubMed:27906160, PubMed:27906161). Contacts proteins S8 and S17. Interacts with ArfA (PubMed:27906160, PubMed:27906161). May interact with IF1 in the 30S initiation complex (By similarity).By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rimPP0A8A83EBI-543960,EBI-561065

Protein-protein interaction databases

BioGridi852156. 1 interactor.
DIPiDIP-35806N.
IntActiP0A7S3. 27 interactors.
STRINGi316385.ECDH10B_p2.

Structurei

Secondary structure

1124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Turni24 – 26Combined sources3
Beta strandi30 – 36Combined sources7
Beta strandi37 – 40Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi52 – 57Combined sources6
Turni58 – 60Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi69 – 71Combined sources3
Beta strandi79 – 84Combined sources6
Beta strandi90 – 92Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi99 – 101Combined sources3
Turni114 – 118Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-L2-124[»]
1MJ1electron microscopy13.00O5-123[»]
1ZN1electron microscopy14.10L28-124[»]
2YKRelectron microscopy9.80L2-124[»]
3DEGelectron microscopy-D2-124[»]
3EP2electron microscopy-L2-124[»]
3EQ3electron microscopy-L2-124[»]
3EQ4electron microscopy-L2-124[»]
3J0Delectron microscopy11.10I2-124[»]
3J0Eelectron microscopy9.90F2-124[»]
3J9Yelectron microscopy3.90l1-124[»]
3J9Zelectron microscopy3.60SL2-124[»]
3JA1electron microscopy3.60SL2-124[»]
3JBUelectron microscopy3.64L1-124[»]
3JBVelectron microscopy3.32L1-124[»]
3JCDelectron microscopy3.70l1-124[»]
3JCEelectron microscopy3.20l1-124[»]
3JCJelectron microscopy3.70t1-124[»]
3JCNelectron microscopy4.60o1-124[»]
4A2Ielectron microscopy16.50L2-124[»]
4ADVelectron microscopy13.50L2-124[»]
4U1UX-ray2.95AL/CL2-124[»]
4U1VX-ray3.00AL/CL2-124[»]
4U20X-ray2.90AL/CL2-124[»]
4U24X-ray2.90AL/CL2-124[»]
4U25X-ray2.90AL/CL2-124[»]
4U26X-ray2.80AL/CL2-124[»]
4U27X-ray2.80AL/CL2-124[»]
4V47electron microscopy12.30BL2-124[»]
4V48electron microscopy11.50BL2-124[»]
4V4HX-ray3.46AL/CL1-124[»]
4V4QX-ray3.46AL/CL2-124[»]
4V4Velectron microscopy15.00AL23-123[»]
4V4Welectron microscopy15.00AL23-123[»]
4V50X-ray3.22AL/CL2-124[»]
4V52X-ray3.21AL/CL2-124[»]
4V53X-ray3.54AL/CL2-124[»]
4V54X-ray3.30AL/CL2-124[»]
4V55X-ray4.00AL/CL2-124[»]
4V56X-ray3.93AL/CL2-124[»]
4V57X-ray3.50AL/CL2-124[»]
4V5BX-ray3.74BL/DL2-124[»]
4V5Helectron microscopy5.80AL2-124[»]
4V5YX-ray4.45AL/CL2-124[»]
4V64X-ray3.50AL/CL2-124[»]
4V65electron microscopy9.00AD1-124[»]
4V66electron microscopy9.00AD1-124[»]
4V69electron microscopy6.70AL2-124[»]
4V6CX-ray3.19AL/CL1-124[»]
4V6DX-ray3.81AL/CL1-124[»]
4V6EX-ray3.71AL/CL1-124[»]
4V6Kelectron microscopy8.25BP1-124[»]
4V6Lelectron microscopy13.20AP1-124[»]
4V6Melectron microscopy7.10AL2-124[»]
AO2-89[»]
4V6Nelectron microscopy12.10BO2-124[»]
4V6Oelectron microscopy14.70AO2-124[»]
4V6Pelectron microscopy13.50AO2-124[»]
4V6Qelectron microscopy11.50AO2-124[»]
4V6Relectron microscopy11.50AO2-124[»]
4V6Selectron microscopy13.10BN2-124[»]
4V6Telectron microscopy8.30AL2-124[»]
4V6Velectron microscopy9.80AL2-124[»]
4V6Yelectron microscopy12.00AL1-124[»]
4V6Zelectron microscopy12.00AL1-124[»]
4V70electron microscopy17.00AL1-124[»]
4V71electron microscopy20.00AL1-124[»]
4V72electron microscopy13.00AL1-124[»]
4V73electron microscopy15.00AL1-124[»]
4V74electron microscopy17.00AL1-124[»]
4V75electron microscopy12.00AL1-124[»]
4V76electron microscopy17.00AL1-124[»]
4V77electron microscopy17.00AL1-124[»]
4V78electron microscopy20.00AL1-124[»]
4V79electron microscopy15.00AL1-124[»]
4V7Aelectron microscopy9.00AL1-124[»]
4V7Belectron microscopy6.80AL1-124[»]
4V7Celectron microscopy7.60AL2-124[»]
4V7Delectron microscopy7.60BL2-124[»]
4V7Ielectron microscopy9.60BL1-124[»]
4V7SX-ray3.25AL/CL2-124[»]
4V7TX-ray3.19AL/CL2-124[»]
4V7UX-ray3.10AL/CL2-124[»]
4V7VX-ray3.29AL/CL2-124[»]
4V85X-ray3.20L1-124[»]
4V89X-ray3.70AL1-124[»]
4V9CX-ray3.30AL/CL1-124[»]
4V9DX-ray3.00AL/BL2-124[»]
4V9OX-ray2.90BL/DL/FL/HL1-124[»]
4V9PX-ray2.90BL/DL/FL/HL1-124[»]
4WF1X-ray3.09AL/CL2-124[»]
4WOIX-ray3.00AL/DL1-124[»]
4WWWX-ray3.10QL/XL2-124[»]
4YBBX-ray2.10AL/BL2-124[»]
5AFIelectron microscopy2.90l1-124[»]
5H5Uelectron microscopy3.00s2-124[»]
5IQRelectron microscopy3.00q1-124[»]
5IT8X-ray3.12AL/BL2-124[»]
5J5BX-ray2.80AL/BL2-124[»]
5J7LX-ray3.00AL/BL2-124[»]
5J88X-ray3.32AL/BL2-124[»]
5J8AX-ray3.10AL/BL2-124[»]
5J91X-ray2.96AL/BL2-124[»]
5JC9X-ray3.03AL/BL2-124[»]
5JTEelectron microscopy3.60AL1-124[»]
5JU8electron microscopy3.60AL1-124[»]
5KCRelectron microscopy3.601l1-124[»]
5KCSelectron microscopy3.901l1-124[»]
5KPSelectron microscopy3.90171-124[»]
5KPVelectron microscopy4.10161-124[»]
5KPWelectron microscopy3.90161-124[»]
5KPXelectron microscopy3.90161-124[»]
5L3Pelectron microscopy3.70l1-124[»]
5LZAelectron microscopy3.60l2-124[»]
5LZBelectron microscopy5.30l2-124[»]
5LZCelectron microscopy4.80l2-124[»]
5LZDelectron microscopy3.40l2-124[»]
5LZEelectron microscopy3.50l2-124[»]
5LZFelectron microscopy4.60l2-124[»]
5MDVelectron microscopy2.97q1-124[»]
5MDWelectron microscopy3.06q1-124[»]
5MDYelectron microscopy3.35q1-124[»]
5MDZelectron microscopy3.10q1-124[»]
5ME0electron microscopy13.50L2-124[»]
5ME1electron microscopy13.50L2-124[»]
5MGPelectron microscopy3.10l2-124[»]
5MY1electron microscopy7.60L2-124[»]
5NO2electron microscopy5.16L2-15[»]
5NO3electron microscopy5.16L2-15[»]
5NO4electron microscopy5.16L2-15[»]
5NP6electron microscopy3.60O2-124[»]
5U4Ielectron microscopy3.50l2-124[»]
5U4Jelectron microscopy3.70l1-124[»]
5U9Felectron microscopy3.20L1-124[»]
5U9Gelectron microscopy3.20L1-124[»]
5UYKelectron microscopy3.90L2-124[»]
5UYLelectron microscopy3.60L2-124[»]
5UYMelectron microscopy3.20L2-124[»]
5UYNelectron microscopy4.00L2-124[»]
5UYPelectron microscopy3.90L2-124[»]
5UYQelectron microscopy3.80L2-124[»]
DisProtiDP00145.
ProteinModelPortaliP0A7S3.
SMRiP0A7S3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7S3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0048. LUCA.
HOGENOMiHOG000040063.
InParanoidiP0A7S3.
KOiK02950.
PhylomeDBiP0A7S3.

Family and domain databases

CDDicd03368. Ribosomal_S12. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B. 1 hit.
InterProiView protein in InterPro
IPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiView protein in Pfam
PF00164. Ribosom_S12_S23. 1 hit.
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00055. RIBOSOMAL_S12. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A7S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR
60 70 80 90 100
KVCRVRLTNG FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG
110 120
ALDCSGVKDR KQARSKYGVK RPKA
Length:124
Mass (Da):13,737
Last modified:January 23, 2007 - v2
Checksum:i94A57F4C4FF0FC5E
GO

Mass spectrometryi

Molecular mass is 13651.3 Da from positions 2 - 124. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti43K → R Confers streptomycin resistance but not hyperaccurate translation. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00355 Genomic DNA. Translation: CAA23648.1.
U18997 Genomic DNA. Translation: AAA58139.1.
U00096 Genomic DNA. Translation: AAC76367.1.
AP009048 Genomic DNA. Translation: BAE77949.1.
AF312716 Genomic DNA. Translation: AAG30936.1.
AF312717 Genomic DNA. Translation: AAG30937.1.
V00354 Genomic DNA. Translation: CAA23647.1.
J01688 Genomic DNA. Translation: AAA50988.1.
PIRiS13738. R3EC12.
RefSeqiNP_417801.1. NC_000913.3.
WP_000246815.1. NZ_CP011343.2.

Genome annotation databases

EnsemblBacteriaiAAC76367; AAC76367; b3342.
BAE77949; BAE77949; BAE77949.
GeneIDi32444591.
947845.
KEGGiecj:JW3304.
eco:b3342.
PATRICifig|1411691.4.peg.3389.

Similar proteinsi

Entry informationi

Entry nameiRS12_ECOLI
AccessioniPrimary (citable) accession number: P0A7S3
Secondary accession number(s): P02367, Q2M707, Q9F5N3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 140 of the entry and version 2 of the sequence. See 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