Reviewed, UniProtKB/Swiss-Prot Q5SHN3 (RS12_THET8)

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) [Complete 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 MF_00403 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 MF_00403
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

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing
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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 132

131

30S ribosomal protein S12 HAMAP MF_00403

PRO_0000146341

Amino acid modifications

Modified residue

89

1

3-methylthioaspartic acid HAMAP MF_00403

Secondary structure

1

.

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132

Helix Strand Turn

Details...

Helix

4 – 10

7

Turn

24 – 26

3

Beta strand

30 – 36

7

Beta strand

50 – 57

8

Beta strand

62 – 66

5

Beta strand

80 – 82

3

Beta strand

95 – 97

3

Turn

115 – 118

4

Helix

123 – 125

3

Sequences

	Sequence		Length	Mass (Da)
	Q5SHN3-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9943D095FAD4D9BC	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

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: 2362824] [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].
[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: 7957245] [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: 16287167] [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: 11014182] [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: 11007480] [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: 11163189] [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: 11014183] [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: 11511350] [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: 11296217] [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: 11228145] [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: 11283358] [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: 11340196] [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: 11866529] [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.

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	1-132	[»]
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	1-125	[»]
1PN8	electron microscopy	10.80	O	1-125	[»]
1PNS	X-ray	8.70	L	2-125	[»]
1PNX	X-ray	9.50	L	2-125	[»]
1QZC	electron microscopy	9.00	L	2-132	[»]
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	1-132	[»]
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	2-131	[»]
2UUB	X-ray	2.90	L	2-131	[»]
2UUC	X-ray	3.10	L	2-131	[»]
2UXB	X-ray	3.10	L	2-131	[»]
2UXC	X-ray	2.90	L	2-131	[»]
2UXD	X-ray	3.20	L	2-131	[»]
2V46	X-ray	3.80	L	2-131	[»]
2V48	X-ray	3.80	L	2-131	[»]
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	[»]
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	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SHN3.

Genome annotation databases

GeneID

3169892.

GenomeReviews

Gene locus TTHA1697 in contig AP008226_GR.

KEGG

ttj:TTHA1697.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0048.

HOGENOM

HBG747181.

OMA

RCEATIN.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1697-MONOMER.

Family and domain databases

HAMAP

MF_00403_B. Ribosomal_S12_B.
[Tree]

InterPro

IPR016027. NA-bd_OB-fold-like.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac-type.
[Graphical view]

PANTHER

PTHR11652:SF1. Ribosom_S12_bac. 1 hit.
PTHR11652. Ribosomal_S12_23. 1 hit.

Pfam

PF00164. Ribosomal_S12. 1 hit.
[Graphical view]

PIRSF

PIRSF002133. Ribosomal_S12/S23. 1 hit.

PRINTS

PR01034. RIBOSOMALS12.

TIGRFAMs

TIGR00981. rpsL_bact. 1 hit.

PROSITE

PS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	February 9, 2010
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)