P0A7V0 (RS2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S2

Gene names

Name:	rpsB
Ordered Locus Names:	b0169, JW0164

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	241 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)

Subunit structure	Part of the 30S ribosomal subunit. Some nascent polypeptide chains are able to cross-link to this protein in situ.
Sequence similarities	Belongs to the ribosomal protein S2P family.
Mass spectrometry	Molecular mass is 26610.5 Da from positions 2 - 241. Determined by MALDI. Ref.12

Ontologies

Keywords
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	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4587209. Source: EcoliWiki
Molecular_function	structural constituent of ribosome Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay PubMed 11985624. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hslR	P0ACG8	2	EBI-543439,EBI-562824

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7 Ref.8

Chain

2 – 241

240

30S ribosomal protein S2 HAMAP-Rule MF_00291_B

PRO_0000134165

Amino acid modifications

Modified residue

115

1

N6-succinyllysine Ref.14

Secondary structure

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241

Helix Strand Turn

Details...

Turn

10 – 15

6

Beta strand

19 – 21

3

Helix

25 – 30

6

Beta strand

31 – 33

3

Helix

35 – 37

3

Beta strand

38 – 40

3

Turn

43 – 45

3

Helix

47 – 49

3

Turn

50 – 52

3

Helix

53 – 62

10

Beta strand

67 – 70

4

Turn

74 – 82

9

Helix

83 – 86

4

Beta strand

87 – 89

3

Beta strand

90 – 92

3

Beta strand

98 – 101

4

Turn

102 – 107

6

Helix

108 – 118

11

Beta strand

121 – 125

5

Beta strand

127 – 129

3

Turn

131 – 137

7

Helix

138 – 145

8

Beta strand

146 – 153

8

Beta strand

162 – 165

4

Helix

167 – 169

3

Helix

170 – 179

10

Beta strand

184 – 186

3

Beta strand

189 – 191

3

Helix

193 – 195

3

Beta strand

197 – 199

3

Beta strand

204 – 206

3

Helix

207 – 218

12

Turn

219 – 221

3

Turn

222 – 224

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7V0 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 87A38C696115212E	FASTA	241	26,744
	10 20 30 40 50 60 MATVSMRDML KAGVHFGHQT RYWNPKMKPF IFGARNKVHI INLEKTVPMF NEALAELNKI 70 80 90 100 110 120 ASRKGKILFV GTKRAASEAV KDAALSCDQF FVNHRWLGGM LTNWKTVRQS IKRLKDLETQ 130 140 150 160 170 180 SQDGTFDKLT KKEALMRTRE LEKLENSLGG IKDMGGLPDA LFVIDADHEH IAIKEANNLG 190 200 210 220 230 240 IPVFAIVDTN SDPDGVDFVI PGNDDAIRAV TLYLGAVAAT VREGRSQDLA SQAEESFVEA E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts." An G., Bendiak D.S., Mamelak L.A., Friesen J.D. Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"Primary structure of protein S2 from the Escherichia coli ribosome." Wittmann-Liebold B., Bosserhoff A. FEBS Lett. 129:10-16(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-241. Strain: K12.
[7]	"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit." Ueshima R., Fujita N., Ishihama A. Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-35, CROSS-LINKING TO RRNA. Strain: MRE-600.
[10]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[11]	"Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit." Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R. Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
[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]	"Identification of lysine succinylation as a new post-translational modification." Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y. Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-115. Strain: K12.
[15]	"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). Strain: MRE-600.
[16]	"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. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.

PIR

R3EC2. A02696.

RefSeq

NP_414711.1. NC_000913.2.
YP_488471.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	B	6-214	[»]
1P87	electron microscopy	11.50	B	2-241	[»]
1VS5	X-ray	3.46	B	1-241	[»]
1VS7	X-ray	3.46	B	1-241	[»]
2AVY	X-ray	3.46	B	2-241	[»]
2AW7	X-ray	3.46	B	2-241	[»]
2GY9	electron microscopy	15.00	B	6-240	[»]
2GYB	electron microscopy	15.00	B	6-240	[»]
2I2P	X-ray	3.22	B	2-240	[»]
2I2U	X-ray	3.22	B	2-240	[»]
2QAL	X-ray	3.21	B	2-241	[»]
2QAN	X-ray	3.21	B	2-241	[»]
2QB9	X-ray	3.54	B	2-241	[»]
2QBB	X-ray	3.54	B	2-241	[»]
2QBD	X-ray	3.30	B	2-241	[»]
2QBF	X-ray	3.30	B	2-241	[»]
2QBH	X-ray	4.00	B	2-241	[»]
2QBJ	X-ray	4.00	B	2-241	[»]
2QOU	X-ray	3.93	B	2-241	[»]
2QOW	X-ray	3.93	B	2-241	[»]
2QOY	X-ray	3.50	B	2-241	[»]
2QP0	X-ray	3.50	B	2-241	[»]
2VHO	X-ray	3.74	B	2-241	[»]
2VHP	X-ray	3.74	B	2-241	[»]
2WWL	electron microscopy	5.80	B	9-226	[»]
2YKR	electron microscopy	9.80	B	9-226	[»]
2Z4K	X-ray	4.45	B	2-241	[»]
2Z4M	X-ray	4.45	B	2-241	[»]
3DF1	X-ray	3.50	B	2-240	[»]
3DF3	X-ray	3.50	B	2-240	[»]
3E1A	electron microscopy	-	B	1-241	[»]
3E1C	electron microscopy	-	B	1-241	[»]
3FIH	electron microscopy	6.70	B	9-226	[»]
3I1M	X-ray	3.19	B	1-241	[»]
3I1O	X-ray	3.19	B	1-241	[»]
3I1Q	X-ray	3.81	B	1-241	[»]
3I1S	X-ray	3.81	B	1-241	[»]
3I1Z	X-ray	3.71	B	1-241	[»]
3I21	X-ray	3.71	B	1-241	[»]
3IZV	electron microscopy	-	F	1-241	[»]
3IZW	electron microscopy	-	F	1-241	[»]
3J00	electron microscopy	-	B	2-241	[»]
3J0U	electron microscopy	12.10	E	2-241	[»]
3J0V	electron microscopy	14.70	E	2-241	[»]
3J0X	electron microscopy	13.50	E	2-241	[»]
3J0Z	electron microscopy	11.50	E	2-241	[»]
3J10	electron microscopy	11.50	E	2-241	[»]
3J13	electron microscopy	13.10	D	2-241	[»]
3J18	electron microscopy	8.30	B	9-226	[»]
3KC4	electron microscopy	-	B	1-241	[»]
3OAQ	X-ray	3.25	B	9-226	[»]
3OAR	X-ray	3.25	B	9-226	[»]
3OFA	X-ray	3.19	B	9-226	[»]
3OFB	X-ray	3.19	B	9-226	[»]
3OFO	X-ray	3.10	B	9-226	[»]
3OFP	X-ray	3.10	B	9-226	[»]
3OFX	X-ray	3.29	B	9-226	[»]
3OFY	X-ray	3.29	B	9-226	[»]
3OR9	X-ray	3.30	B	1-241	[»]
3ORA	X-ray	3.30	B	1-241	[»]
3SFS	X-ray	3.20	B	1-241	[»]
3UOQ	X-ray	3.70	B	1-241	[»]
4A2I	electron microscopy	16.50	B	9-226	[»]
4ADV	electron microscopy	13.50	B	2-241	[»]
4GAQ	X-ray	3.30	B	1-241	[»]
4GAS	X-ray	3.30	B	1-241	[»]
4GD1	X-ray	3.00	B	9-226	[»]
4GD2	X-ray	3.00	B	9-226	[»]

ProteinModelPortal

P0A7V0.

SMR

P0A7V0. Positions 2-241.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7V0. 206 interactions.

STRING

511145.b0169.

2D gel databases

SWISS-2DPAGE

P0A7V0.

Proteomic databases

PaxDb

P0A7V0.

PRIDE

P0A7V0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.

GeneID

12931818.
947874.

KEGG

ecj:Y75_p0165.
eco:b0169.

PATRIC

32115445. VBIEscCol129921_0174.

Organism-specific databases

EchoBASE

EB0894.

EcoGene

EG10901. rpsB.

Phylogenomic databases

eggNOG

COG0052.

HOGENOM

HOG000071892.

KO

K02967.

OMA

NVAGGTD.

ProtClustDB

PRK05299.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.

Gene expression databases

Genevestigator

P0A7V0.

Family and domain databases

HAMAP

MF_00291_B. Ribosomal_S2_B.

InterPro

IPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]

PANTHER

PTHR12534. PTHR12534. 1 hit.

Pfam

PF00318. Ribosomal_S2. 1 hit.
[Graphical view]

PRINTS

PR00395. RIBOSOMALS2.

SUPFAM

SSF52313. Ribosomal_S2. 1 hit.

TIGRFAMs

TIGR01011. rpsB_bact. 1 hit.

PROSITE

PS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1922.

EvolutionaryTrace

P0A7V0.

Entry information

Entry name

RS2_ECOLI

Accession

Primary (citable) accession number: P0A7V0
Secondary accession number(s): P02351, Q9R2E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program