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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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.11

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 direct assay. Source: EcoliWiki
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay. Source: EcoliWiki
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural constituent of ribosome Inferred from direct assay. Source: EcoliWiki zinc ion binding Inferred from direct assay. 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 MF_00291_B

PRO_0000134165

Secondary structure

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241

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Helix

43 – 45

3

Helix

47 – 61

15

Turn

62 – 64

3

Beta strand

68 – 70

3

Helix

74 – 77

4

Turn

78 – 80

3

Helix

81 – 84

4

Turn

85 – 87

3

Beta strand

89 – 92

4

Beta strand

100 – 102

3

Helix

104 – 122

19

Helix

124 – 126

3

Helix

131 – 147

17

Turn

148 – 153

6

Beta strand

161 – 164

4

Turn

166 – 169

4

Helix

170 – 179

10

Beta strand

183 – 185

3

Helix

193 – 195

3

Beta strand

197 – 199

3

Helix

207 – 222

16

Turn

223 – 225

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: 6272196] [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: 8202364] [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: 9278503] [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: 16738553] [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: 7023985] [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: 1575737] [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: 9298646] [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: 7556101] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-35, CROSS-LINKING TO RRNA. Strain: MRE-600.
[10]	"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: 9716382] [Abstract] Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
[11]	"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: 10094780] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[12]	"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: 12244297] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[13]	"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: 12809609] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[14]	"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: 16272117] [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.

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	[»]
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	[»]
3R8N	X-ray	3.00	B	9-226	[»]
3R8O	X-ray	3.00	B	9-226	[»]
4A2I	electron microscopy	16.50	B	9-226	[»]

ProteinModelPortal

P0A7V0.

SMR

P0A7V0. Positions 2-241.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7V0. 205 interactions.

2D gel databases

SWISS-2DPAGE

P0A7V0.

ECO2DBASE

H027.0. 6TH EDITION.

Proteomic databases

PRIDE

P0A7V0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000658; EBESCP00000000658; EBESCG00000000549.
EBESCT00000016914; EBESCP00000016205; EBESCG00000015973.

GeneID

947874.

GenomeReviews

Gene locus JW0164 in contig AP009048_GR.
Gene locus b0169 in contig U00096_GR.

KEGG

ecj:JW0164.
eco:b0169.

PATRIC

32115445. VBIEscCol129921_0174.

Organism-specific databases

EchoBASE

EB0894.

EcoGene

EG10901. rpsB.

Phylogenomic databases

eggNOG

COG0052.

GeneTree

EBGT00050000011931.

HOGENOM

HBG736296.

OMA

INLYLNI.

PhylomeDB

P0A7V0.

ProtClustDB

PRK05299.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10901-MONOMER.

Gene expression databases

Genevestigator

P0A7V0.

Family and domain databases

HAMAP

MF_00291_B. Ribosomal_S2_B.
[Tree]

InterPro

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

KO

K02967.

PANTHER

PTHR12534. Ribosom_S2_bac. 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...

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:	January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program