30S ribosomal protein S12 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q5SHN3 (RS12_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
30S ribosomal protein S12

Gene names

Name:	rpsL
Ordered Locus Names:	TTHA1697

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length	132 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	With S4 and S5 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_00403_B 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. HAMAP-Rule MF_00403_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14
Sequence similarities	Belongs to the ribosomal protein S12P family.
Mass spectrometry	Molecular mass is 14516 Da from positions 2 - 132. Determined by MALDI. Ref.4
Sequence caution	The sequence BAD71520.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA36418.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	small ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 132

131

30S ribosomal protein S12 HAMAP-Rule MF_00403_B

PRO_0000146341

Amino acid modifications

Modified residue

3-methylthioaspartic acid HAMAP-Rule MF_00403_B

Secondary structure

132

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SHN3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9943D095FAD4D9BC
Show »

FASTA

132

14,599

        10         20         30         40         50         60 
MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR KVAKVRLTSG 

        70         80         90        100        110        120 
YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG VYDAAGVKDR KKSRSKYGTK 

       130 
KPKEAAKTAA KK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes coding for the ribosomal proteins S12 and S7." Yakhnin A.V., Vorozheykina D.P., Matvienko N.I. Nucleic Acids Res. 18:3659-3659(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[3]	"Purification and characterization of the 30S ribosomal proteins from the bacterium Thermus thermophilus." Tsiboli P., Herfurth E., Choli T. Eur. J. Biochem. 226:169-177(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-29.
[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: BETA-METHYLTHIOLATION AT ASP-89, MASS SPECTROMETRY.
[5]	"Structure of the 30S ribosomal subunit." Wimberly B.T., Brodersen D.E., Clemons W.M. Jr., Morgan-Warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Nature 407:327-339(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
[6]	"Structure of functionally activated small ribosomal subunit at 3.3 A resolution." Schluenzen F., Tocilj A., Zarivach R., Harms J., Gluehmann M., Janell D., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A. Cell 102:615-623(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[7]	"The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit." Brodersen D.E., Clemons W.M. Jr., Carter A.P., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. Cell 103:1143-1154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[8]	"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics." Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. Nature 407:340-348(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 30S SUBUNIT.
[9]	"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 (5.00 ANGSTROMS) OF THE RIBOSOME.
[10]	"Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3." Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H., Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A., Franceschi F. EMBO J. 20:1829-1839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[11]	"Crystal structure of an initiation factor bound to the 30S ribosomal subunit." Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Hartsch T., Wimberly B.T., Ramakrishnan V. Science 291:498-501(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[12]	"Crystal structure of the ribosome at 5.5 A resolution." Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F. Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
[13]	"Recognition of cognate transfer RNA by the 30S ribosomal subunit." Ogle J.M., Brodersen D.E., Clemons W.M. Jr., Tarry M.J., Carter A.P., Ramakrishnan V. Science 292:897-902(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF THE 30S SUBUNIT.
[14]	"Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA." Brodersen D.E., Clemons W.M. Jr., Carter A.P., Wimberly B.T., Ramakrishnan V. J. Mol. Biol. 316:725-768(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
+	Additional computationally mapped references.

Web resources

T.thermophilus ribosome structure and function

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52165 Genomic DNA. Translation: CAA36418.1. Different initiation.
AP008226 Genomic DNA. Translation: BAD71520.1. Different initiation.

PIR

R3TW12. S10249.

RefSeq

YP_144963.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	L	2-132	[»]
1GIX	X-ray	5.50	O	2-132	[»]
1HNW	X-ray	3.40	L	2-132	[»]
1HNX	X-ray	3.40	L	2-132	[»]
1HNZ	X-ray	3.30	L	2-132	[»]
1HR0	X-ray	3.20	L	2-132	[»]
1I94	X-ray	3.20	L	2-132	[»]
1I95	X-ray	4.50	L	2-132	[»]
1I96	X-ray	4.20	L	2-132	[»]
1I97	X-ray	4.50	L	2-132	[»]
1IBK	X-ray	3.31	L	2-132	[»]
1IBL	X-ray	3.11	L	2-132	[»]
1IBM	X-ray	3.31	L	2-132	[»]
1J5E	X-ray	3.05	L	2-132	[»]
1JGO	X-ray	5.60	O	2-132	[»]
1JGP	X-ray	7.00	O	2-132	[»]
1JGQ	X-ray	5.00	O	2-132	[»]
1L1U	model	-	L	1-125	[»]
1MVR	electron microscopy	12.80	O	2-131	[»]
1N32	X-ray	3.00	L	2-132	[»]
1N33	X-ray	3.35	L	2-132	[»]
1N34	X-ray	3.80	L	2-132	[»]
1N36	X-ray	3.65	L	2-132	[»]
1PN7	electron microscopy	10.80	O	2-124	[»]
1PN8	electron microscopy	10.80	O	2-124	[»]
1QZC	electron microscopy	9.00	L	2-131	[»]
1XMO	X-ray	3.25	L	2-132	[»]
1XMQ	X-ray	3.00	L	2-132	[»]
1XNQ	X-ray	3.05	L	2-132	[»]
1XNR	X-ray	3.10	L	2-132	[»]
1YL4	X-ray	5.50	O	2-132	[»]
2B64	X-ray	5.90	L	2-132	[»]
2B9M	X-ray	6.76	L	2-132	[»]
2B9O	X-ray	6.46	L	2-132	[»]
2E5L	X-ray	3.30	L	2-132	[»]
2F4V	X-ray	3.80	L	1-132	[»]
2HGI	X-ray	5.00	O	1-132	[»]
2HGP	X-ray	5.50	O	1-132	[»]
2HGR	X-ray	4.51	O	1-132	[»]
2HHH	X-ray	3.35	L	2-132	[»]
2J00	X-ray	2.80	L	2-131	[»]
2J02	X-ray	2.80	L	2-131	[»]
2OW8	X-ray	3.71	m	-	[»]
2UU9	X-ray	3.10	L	2-131	[»]
2UUA	X-ray	2.90	L	2-132	[»]
2UUB	X-ray	2.90	L	2-131	[»]
2UUC	X-ray	3.10	L	2-131	[»]
2UXB	X-ray	3.10	L	2-132	[»]
2UXC	X-ray	2.90	L	2-132	[»]
2UXD	X-ray	3.20	L	2-132	[»]
2V46	X-ray	3.80	L	2-131	[»]
2V48	X-ray	3.50	L	2-132	[»]
2VQE	X-ray	2.50	L	2-132	[»]
2VQF	X-ray	2.90	L	2-132	[»]
2WDG	X-ray	3.30	L	2-132	[»]
2WDH	X-ray	3.30	L	2-132	[»]
2WDK	X-ray	3.50	L	2-132	[»]
2WDM	X-ray	3.50	L	2-132	[»]
2WH1	X-ray	3.45	L	1-132	[»]
2WH3	X-ray	3.45	L	1-132	[»]
2WRI	X-ray	3.60	L	1-132	[»]
2WRK	X-ray	3.60	L	1-132	[»]
2WRN	X-ray	3.60	L	2-132	[»]
2WRQ	X-ray	3.60	L	2-132	[»]
2X9R	X-ray	3.10	L	1-132	[»]
2X9T	X-ray	3.10	L	1-132	[»]
2XFZ	X-ray	3.20	L	2-132	[»]
2XG1	X-ray	3.20	L	2-132	[»]
2XQD	X-ray	3.10	L	2-132	[»]
2XSY	electron microscopy	7.80	L	1-132	[»]
2XUY	electron microscopy	7.60	L	1-132	[»]
2Y0U	X-ray	3.10	L	2-132	[»]
2Y0W	X-ray	3.10	L	2-132	[»]
2Y0Y	X-ray	3.10	L	1-132	[»]
2Y10	X-ray	3.10	L	2-132	[»]
2Y12	X-ray	3.10	L	2-132	[»]
2Y14	X-ray	3.10	L	2-132	[»]
2Y16	X-ray	3.10	L	2-132	[»]
2Y18	X-ray	3.10	L	2-132	[»]
2ZM6	X-ray	3.30	L	2-132	[»]
3FIC	electron microscopy	6.40	L	2-126	[»]
3HUW	X-ray	3.10	L	1-132	[»]
3HUY	X-ray	3.10	L	1-132	[»]
3I8G	X-ray	3.10	O	1-132	[»]
3I8H	X-ray	3.10	O	1-132	[»]
3I9B	X-ray	3.50	O	1-132	[»]
3I9D	X-ray	3.50	O	1-132	[»]
3KIQ	X-ray	3.30	l	1-132	[»]
3KIS	X-ray	3.30	l	1-132	[»]
3KIU	X-ray	3.60	l	1-132	[»]
3KIX	X-ray	3.60	l	1-132	[»]
3KNH	X-ray	3.00	L	1-132	[»]
3KNJ	X-ray	3.15	L	1-132	[»]
3KNL	X-ray	3.45	L	1-132	[»]
3KNN	X-ray	3.45	L	1-132	[»]
3OGE	X-ray	3.00	L	2-132	[»]
3OGY	X-ray	3.00	L	2-132	[»]
3OHC	X-ray	3.00	L	2-132	[»]
3OHD	X-ray	3.00	L	2-132	[»]
3OHY	X-ray	3.00	L	2-132	[»]
3OI0	X-ray	3.00	L	2-132	[»]
3OI2	X-ray	3.10	L	2-132	[»]
3OI4	X-ray	3.10	L	2-132	[»]
3OTO	X-ray	3.69	L	2-132	[»]
3T1H	X-ray	3.11	L	1-132	[»]
3T1Y	X-ray	2.80	L	1-132	[»]
3TVF	X-ray	3.10	O	1-132	[»]
3TVG	X-ray	3.10	O	1-132	[»]
3UXS	X-ray	3.20	L	1-132	[»]
3UXT	X-ray	3.20	L	1-132	[»]
3UYD	X-ray	3.00	O	1-128	[»]
3UYF	X-ray	3.00	O	1-128	[»]
3UZ3	X-ray	3.30	O	1-132	[»]
3UZ4	X-ray	3.30	O	1-132	[»]
3UZ6	X-ray	3.00	O	1-132	[»]
3UZ7	X-ray	3.00	O	1-132	[»]
3UZG	X-ray	3.30	O	1-132	[»]
3UZI	X-ray	3.30	O	1-132	[»]
3UZL	X-ray	3.30	O	1-128	[»]
3UZM	X-ray	3.30	O	1-128	[»]
3V22	X-ray	3.00	L	1-132	[»]
3V24	X-ray	3.00	L	1-132	[»]
3V26	X-ray	3.10	L	1-132	[»]
3V28	X-ray	3.10	L	1-132	[»]
3V2C	X-ray	2.70	L	1-132	[»]
3V2E	X-ray	2.70	L	1-132	[»]
3ZN7	X-ray	3.10	L	2-132	[»]
3ZND	X-ray	3.10	L	2-132	[»]
3ZVO	X-ray	3.80	L	2-132	[»]
4ABR	X-ray	3.10	L	2-132	[»]
4AQY	X-ray	3.50	L	2-132	[»]
4B8F	X-ray	3.70	L	1-132	[»]
4B8H	X-ray	3.70	L	1-132	[»]
4DH9	X-ray	3.20	L	1-132	[»]
4DHB	X-ray	3.20	L	1-132	[»]
4DUY	X-ray	3.39	L	2-132	[»]
4DUZ	X-ray	3.65	L	2-132	[»]
4DV0	X-ray	3.85	L	2-132	[»]
4DV1	X-ray	3.85	L	2-132	[»]
4DV2	X-ray	3.65	L	2-132	[»]
4DV3	X-ray	3.55	L	2-132	[»]
4DV4	X-ray	3.65	L	2-132	[»]
4DV5	X-ray	3.68	L	2-132	[»]
4DV6	X-ray	3.30	L	2-132	[»]
4DV7	X-ray	3.29	L	2-132	[»]
4G5K	X-ray	3.30	O	1-127	[»]
4G5M	X-ray	3.30	O	1-127	[»]
4G5T	X-ray	3.10	O	1-127	[»]
4G5V	X-ray	3.10	O	1-127	[»]

ProteinModelPortal

Q5SHN3.

SMR

Q5SHN3. Positions 2-126.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1697.

Proteomic databases

PRIDE

Q5SHN3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71520; BAD71520; BAD71520.

GeneID

3169892.

KEGG

ttj:TTHA1697.

PATRIC

23958349. VBITheThe93045_1667.

Phylogenomic databases

eggNOG

COG0048.

HOGENOM

HOG000040063.

K02950.

OMA

ITINQLH.

ProtClustDB

PRK05163.

Enzyme and pathway databases

BioCyc

TTHE300852:GH8R-1736-MONOMER.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

HAMAP

MF_00403_B. Ribosomal_S12_B.

InterPro

IPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]

PANTHER

PTHR11652. PTHR11652. 1 hit.

Pfam

PF00164. Ribosomal_S12. 1 hit.
[Graphical view]

PIRSF

PIRSF002133. Ribosomal_S12/S23. 1 hit.

PRINTS

PR01034. RIBOSOMALS12.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

TIGRFAMs

TIGR00981. rpsL_bact. 1 hit.

PROSITE

PS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHN3.

Entry information

Entry name

RS12_THET8

Accession

Primary (citable) accession number: Q5SHN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents