P0A7S9 (RS13_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S13

Gene names

Name:	rpsM
Ordered Locus Names:	b3298, JW3260

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	118 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	Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. Ref.11 In the E.coli 70S ribosome in the initiation state (Ref.14) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; bridge B1a is broken in the model with bound EF-G, while the protein-protein contacts between S13 and L5 in B1b change (Ref.14). The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (Ref.15), contacting alternately S13 or S19. In the two 3.5 angstroms resolved ribosome structures (Ref.16) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder. Ref.11 Contacts the tRNAs in the A and P sites. Ref.11 The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Ref.11
Subunit structure	Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Cross-links to the P site tRNA and weakly to the A site tRNA. Forms two bridges to the 50S subunit in the 70S ribosome, contacting the 16S rRNA and proteins S19 and L5. Ref.14 Ref.15
Sequence similarities	Belongs to the ribosomal protein S13P family.
Mass spectrometry	Molecular mass is 12968.1 Da from positions 2 - 118. Determined by MALDI. Ref.12

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	ribosome biogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome translation Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4587209. Source: EcoliWiki
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 118

117

30S ribosomal protein S13 HAMAP-Rule MF_01315

PRO_0000132089

Natural variations

Natural variant

89 – 99

11

Missing in PW118; partially suppresses a rimM deletion.

Natural variant

100 – 118

19

Missing in rpsM413; pseudorevertant of streptomycin resistance. A strong antisuppressor of two tRNA suppressors, decreases translation step time and growth rate.

Natural variant

105

1

N → H in PW095; partially suppresses a rimM deletion.

Natural variant

105

1

N → K in PW097; partially suppresses a rimM deletion.

Experimental info

Mutagenesis

83 – 118

36

Missing: Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro.

Mutagenesis

114 – 118

5

Missing: Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro.

Secondary structure

1

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118

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Beta strand

12 – 14

3

Helix

15 – 18

4

Helix

19 – 21

3

Beta strand

22 – 24

3

Helix

27 – 35

9

Turn

36 – 38

3

Beta strand

41 – 43

3

Turn

45 – 47

3

Helix

50 – 57

8

Helix

60 – 62

3

Helix

66 – 83

18

Helix

86 – 93

8

Beta strand

97 – 99

3

Beta strand

102 – 104

3

Helix

107 – 110

4

Sequences

	Sequence		Length	Mass (Da)
	P0A7S9 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6277C365EBE4F732	FASTA	118	13,099
	10 20 30 40 50 60 MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE GQIDTLRDEV 70 80 90 100 110 AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ RTKTNARTRK GPRKPIKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli." Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L. Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Primary structure of protein S13 from the small subunit of Escherichia coli ribosomes." Lindemann H., Wittmann-Liebold B. Hoppe-Seyler's Z. Physiol. Chem. 358:843-863(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-118. Strain: K.
[5]	"DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli." Post L.E., Arfsten A.E., Davis G.R., Nomura M. J. Biol. Chem. 255:4653-4659(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
[6]	"Growth-rate-dependent regulation of ribosome synthesis in E. coli: expression of the lacZ and galK genes fused to ribosomal promoters." Miura A., Krueger J.H., Itoh S., de Boer H.A., Nomura M. Cell 25:773-782(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
[7]	"Identification of a cross-link in the Escherichia coli ribosomal protein pair S13-S19 at the amino acid level." Pohl T., Wittmann-Liebold B. J. Biol. Chem. 263:4293-4301(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-85, CROSS-LINKING TO S19. Strain: K12 / A19.
[8]	"Antisuppression by a mutation in rpsM(S13) giving a shortened ribosomal protein S13." Faxen M., Walles-Granberg A., Isaksson L.A. Biochim. Biophys. Acta 1218:27-34(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT RPSM413. Strain: K12.
[9]	"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site." Osswald M., Doering T., Brimacombe R. Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD. Strain: MRE-600.
[10]	"A novel ribosome-associated protein is important for efficient translation in Escherichia coli." Bylund G.O., Persson B.C., Lundberg L.A., Wikstroem P.M. J. Bacteriol. 179:4567-4574(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ABILITY OF VARIANTS PW118; PW097 AND PW095 TO PARTIALLY SUPPRESS A RIMM DELETION. Strain: MW100.
[11]	"Creating ribosomes with an all-RNA 30S subunit P site." Hoang L., Fredrick K., Noller H.F. Proc. Natl. Acad. Sci. U.S.A. 101:12439-12443(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN P SITE TRNA-BINDING, MUTAGENESIS. Strain: CSH142.
[12]	"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Arnold R.J., Reilly J.P. Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[13]	"All-atom homology model of the Escherichia coli 30S ribosomal subunit." Tung C.-S., Joseph S., Sanbonmatsu K.Y. Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[14]	"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement." Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J. Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION. Strain: MRE-600.
[15]	"Structures of the bacterial ribosome at 3.5 A resolution." Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D. Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE B1B. Strain: MRE-600.
[16]	"Locking and unlocking of ribosomal motions." Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J. Cell 114:123-134(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02543 Genomic DNA. Translation: CAA26392.1.
U18997 Genomic DNA. Translation: AAA58093.1.
U00096 Genomic DNA. Translation: AAC76323.1.
AP009048 Genomic DNA. Translation: BAE77993.1.
M12432 Genomic DNA. Translation: AAA83903.1.
M10213 Genomic DNA. Translation: AAA72457.1.

PIR

R3EC13. A23807.

RefSeq

NP_417757.1. NC_000913.2.
YP_492134.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	M	2-118	[»]
1P6G	electron microscopy	12.30	M	2-118	[»]
1P87	electron microscopy	11.50	M	2-118	[»]
1VS5	X-ray	3.46	M	1-118	[»]
1VS7	X-ray	3.46	M	1-118	[»]
2AVY	X-ray	3.46	M	2-118	[»]
2AW7	X-ray	3.46	M	2-118	[»]
2GY9	electron microscopy	15.00	M	2-115	[»]
2GYB	electron microscopy	15.00	M	2-115	[»]
2I2P	X-ray	3.22	M	2-117	[»]
2I2U	X-ray	3.22	M	2-117	[»]
2QAL	X-ray	3.21	M	2-118	[»]
2QAN	X-ray	3.21	M	2-118	[»]
2QB9	X-ray	3.54	M	2-118	[»]
2QBB	X-ray	3.54	M	2-118	[»]
2QBD	X-ray	3.30	M	2-118	[»]
2QBF	X-ray	3.30	M	2-118	[»]
2QBH	X-ray	4.00	M	2-118	[»]
2QBJ	X-ray	4.00	M	2-118	[»]
2QOU	X-ray	3.93	M	2-118	[»]
2QOW	X-ray	3.93	M	2-118	[»]
2QOY	X-ray	3.50	M	2-118	[»]
2QP0	X-ray	3.50	M	2-118	[»]
2VHO	X-ray	3.74	M	2-118	[»]
2VHP	X-ray	3.74	M	2-118	[»]
2WWL	electron microscopy	5.80	M	2-114	[»]
2YKR	electron microscopy	9.80	M	2-115	[»]
2Z4K	X-ray	4.45	M	2-118	[»]
2Z4M	X-ray	4.45	M	2-118	[»]
3DF1	X-ray	3.50	M	2-117	[»]
3DF3	X-ray	3.50	M	2-117	[»]
3E1A	electron microscopy	-	F	1-118	[»]
3E1C	electron microscopy	-	F	1-118	[»]
3FIH	electron microscopy	6.70	M	2-114	[»]
3I1M	X-ray	3.19	M	1-118	[»]
3I1O	X-ray	3.19	M	1-118	[»]
3I1Q	X-ray	3.81	M	1-118	[»]
3I1S	X-ray	3.81	M	1-118	[»]
3I1Z	X-ray	3.71	M	1-118	[»]
3I21	X-ray	3.71	M	1-118	[»]
3IZV	electron microscopy	-	Q	1-118	[»]
3IZW	electron microscopy	-	Q	1-118	[»]
3J00	electron microscopy	-	M	2-118	[»]
3J0U	electron microscopy	12.10	P	2-118	[»]
3J0V	electron microscopy	14.70	P	2-118	[»]
3J0X	electron microscopy	13.50	P	2-118	[»]
3J0Z	electron microscopy	11.50	P	2-118	[»]
3J10	electron microscopy	11.50	P	2-118	[»]
3J13	electron microscopy	13.10	O	2-118	[»]
3J18	electron microscopy	8.30	M	2-115	[»]
3J36	electron microscopy	9.80	M	2-118	[»]
3KC4	electron microscopy	-	M	1-118	[»]
3OAQ	X-ray	3.25	M	2-115	[»]
3OAR	X-ray	3.25	M	2-114	[»]
3OFA	X-ray	3.19	M	2-115	[»]
3OFB	X-ray	3.19	M	2-114	[»]
3OFO	X-ray	3.10	M	2-115	[»]
3OFP	X-ray	3.10	M	2-114	[»]
3OFX	X-ray	3.29	M	2-115	[»]
3OFY	X-ray	3.29	M	2-114	[»]
3OR9	X-ray	3.30	M	1-118	[»]
3ORA	X-ray	3.30	M	1-118	[»]
3SFS	X-ray	3.20	M	1-118	[»]
3UOQ	X-ray	3.70	M	1-118	[»]
4A2I	electron microscopy	16.50	M	2-115	[»]
4ADV	electron microscopy	13.50	M	2-118	[»]
4GAQ	X-ray	3.30	M	1-118	[»]
4GAS	X-ray	3.30	M	1-118	[»]
4GD1	X-ray	3.00	M	2-115	[»]
4GD2	X-ray	3.00	M	2-115	[»]
4KIY	X-ray	2.90	M	1-118	[»]
4KJ0	X-ray	2.90	M	1-118	[»]
4KJ2	X-ray	2.90	M	1-118	[»]
4KJ4	X-ray	2.90	M	1-118	[»]
4KJ6	X-ray	2.90	M	1-118	[»]
4KJ8	X-ray	2.90	M	1-118	[»]
4KJA	X-ray	2.90	M	1-118	[»]
4KJC	X-ray	2.90	M	1-118	[»]

ProteinModelPortal

P0A7S9.

SMR

P0A7S9. Positions 2-116.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35855N.

IntAct

P0A7S9. 101 interactions.

MINT

MINT-1290225.

STRING

511145.b3298.

Proteomic databases

PaxDb

P0A7S9.

PRIDE

P0A7S9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76323; AAC76323; b3298.
BAE77993; BAE77993; BAE77993.

GeneID

12934445.
947791.

KEGG

ecj:Y75_p3878.
eco:b3298.

PATRIC

32122028. VBIEscCol129921_3391.

Organism-specific databases

EchoBASE

EB0905.

EcoGene

EG10912. rpsM.

Phylogenomic databases

eggNOG

COG0099.

HOGENOM

HOG000039879.

KO

K02952.

OMA

REVAMNI.

OrthoDB

EOG618R01.

ProtClustDB

PRK05179.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10912-MONOMER.
ECOL316407:JW3260-MONOMER.

Gene expression databases

Genevestigator

P0A7S9.

Family and domain databases

Gene3D

4.10.910.10. 1 hit.

HAMAP

MF_01315. Ribosomal_S13/S18.

InterPro

IPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR019980. Ribosomal_S13_bac-type.
IPR018269. Ribosomal_S13_CS.
[Graphical view]

Pfam

PF00416. Ribosomal_S13. 1 hit.
[Graphical view]

PIRSF

PIRSF002134. Ribosomal_S13. 1 hit.

SUPFAM

SSF46946. SSF46946. 1 hit.

TIGRFAMs

TIGR03631. bact_S13. 1 hit.

PROSITE

PS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2363135.

EvolutionaryTrace

P0A7S9.

PRO

P0A7S9.

Entry information

Entry name

RS13_ECOLI

Accession

Primary (citable) accession number: P0A7S9
Secondary accession number(s): P02369, Q2M6W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 13, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program