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Protein

30S ribosomal protein S12

Gene

rpsL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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 similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU01100-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S12
Short name:
BS12
Gene namesi
Name:rpsL
Synonyms:fun, strA
Ordered Locus Names:BSU01100
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → D: Confers streptomycin resistance and very poor growth in rich medium. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 13813730S ribosomal protein S12PRO_0000146178Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei102 – 1021Not modifiedCurated

Proteomic databases

PaxDbiP21472.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex (By similarity).By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000570.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Welectron microscopy3.90AL1-138[»]
ProteinModelPortaliP21472.
SMRiP21472. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiENOG4108UKE. Bacteria.
COG0048. LUCA.
HOGENOMiHOG000040063.
InParanoidiP21472.
KOiK02950.
OMAiLKSCPER.
OrthoDBiEOG61ZTNF.
PhylomeDBiP21472.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21472-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTINQLIRK GRVSKVENSK SPALNKGYNS FKKEHTNVSS PQKRGVCTRV
60 70 80 90 100
GTMTPKKPNS ALRKYARVRL TNGIEVTAYI PGIGHNLQEH SVVLIRGGRV
110 120 130
KDLPGVRYHI VRGALDTAGV ENRAQGRSKY GTKKPKAK
Length:138
Mass (Da):15,216
Last modified:June 16, 2009 - v5
Checksum:i1E8EDCEC75B75648
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021D → N in BAA11001 (PubMed:8969501).Curated
Sequence conflicti105 – 1051G → R in BAA11001 (PubMed:8969501).Curated
Sequence conflicti128 – 1281S → P in BAA11001 (PubMed:8969501).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561K → I in RPSL4 (STRA1); confers streptomycin resistance and hyperaccurate translation, has no effect on natural antibiotic production.
Natural varianti56 – 561K → R in RPSL1 (KO-267); confers streptomycin resistance but not hyperaccurate translation, increases natural antibiotic production 10-fold.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64127 Genomic DNA. Translation: BAA11001.1.
AL009126 Genomic DNA. Translation: CAB11886.2.
L43593 Genomic DNA. Translation: AAB59114.1.
PIRiC69700.
RefSeqiNP_387991.2. NC_000964.3.
WP_003225781.1. NZ_JNCM01000029.1.

Genome annotation databases

EnsemblBacteriaiCAB11886; CAB11886; BSU01100.
GeneIDi11237879.
936616.
KEGGibsu:BSU01100.
PATRICi18971729. VBIBacSub10457_0113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64127 Genomic DNA. Translation: BAA11001.1.
AL009126 Genomic DNA. Translation: CAB11886.2.
L43593 Genomic DNA. Translation: AAB59114.1.
PIRiC69700.
RefSeqiNP_387991.2. NC_000964.3.
WP_003225781.1. NZ_JNCM01000029.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Welectron microscopy3.90AL1-138[»]
ProteinModelPortaliP21472.
SMRiP21472. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000570.

Proteomic databases

PaxDbiP21472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11886; CAB11886; BSU01100.
GeneIDi11237879.
936616.
KEGGibsu:BSU01100.
PATRICi18971729. VBIBacSub10457_0113.

Phylogenomic databases

eggNOGiENOG4108UKE. Bacteria.
COG0048. LUCA.
HOGENOMiHOG000040063.
InParanoidiP21472.
KOiK02950.
OMAiLKSCPER.
OrthoDBiEOG61ZTNF.
PhylomeDBiP21472.

Enzyme and pathway databases

BioCyciBSUB:BSU01100-MONOMER.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus subtilis chromosome."
    Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K., Kawamura F., Yoshikawa H., Takahashi H.
    Microbiology 142:3039-3046(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. Ochi K., Takashi I., Forbes A., Kelleher N.L., Garavelli J.S.
    Unpublished observations (AUG-2002)
    Cited for: SEQUENCE REVISION TO 102; 105 AND 128, ABSENCE OF MODIFICATION.
    Strain: 168.
  4. "Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12."
    Carr J.F., Hamburg D.M., Gregory S.T., Limbach P.A., Dahlberg A.E.
    J. Bacteriol. 188:2020-2023(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 102 AND 105.
    Strain: 168 / BGSC1A1 and ATCC 21332 / IAM 1213.
  5. "B. subtilis ribosomal proteins: structural homology and post-translational modifications."
    Lauber M.A., Running W.E., Reilly J.P.
    J. Proteome Res. 8:4193-4206(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 102; 105 AND 128, ABSENCE OF MODIFICATION.
    Strain: 168.
  6. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 102; 105 AND 128.
  7. "Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase."
    Boor K.J., Duncan M.L., Price C.W.
    J. Biol. Chem. 270:20329-20336(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  8. "Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: correlation to Escherichia coli 30S proteins."
    Higo K., Otaka E., Osawa S.
    Mol. Gen. Genet. 185:239-244(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
  9. "Acquisition of certain streptomycin-resistant (str) mutations enhances antibiotic production in bacteria."
    Hosoya Y., Okamoto S., Muramatsu H., Ochi K.
    Antimicrob. Agents Chemother. 42:2041-2047(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS STREPTOMYCIN RESISTANT, ANTIBIOTIC PRODUCTION.
    Strain: 168.
  10. "Construction of an in vivo nonsense readthrough assay system and functional analysis of ribosomal proteins S12, S4, and S5 in Bacillus subtilis."
    Inaoka T., Kasai K., Ochi K.
    J. Bacteriol. 183:4958-4963(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS, VARIANTS STREPTOMYCIN RESISTANT.
    Strain: 168.

Entry informationi

Entry nameiRS12_BACSU
AccessioniPrimary (citable) accession number: P21472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 16, 2009
Last modified: April 13, 2016
This is version 134 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Many streptomycin resistant B.subtilis with mutations in this protein produce increased quantities of a natural (but uncharacterized) antibiotic.
A number of substitutions and deletions can promote streptomycin resistance, dependence or pseudodependence; all but one of these (K55R) are associated with hyperaccurate translation.

Caution

The enzyme that would modify Asp-102 to 3-methylthioaspartic acid has not been found in the proteome of this organism, and that modification does not occur.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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

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 one 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.