P0A7U3 (RS19_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S19

Gene names

Name:	rpsS
Ordered Locus Names:	b3316, JW3278

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	92 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	In the E.coli 70S ribosome in the initiation state (Ref.10) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (Ref.11), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (Ref.12) 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. HAMAP-Rule MF_00531 Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA. HAMAP-Rule MF_00531
Subunit structure	Part of the 30S ribosomal subunit. Binds S13 and L5 and cross-links to the A site tRNA. Ref.10 Ref.12
Sequence similarities	Belongs to the ribosomal protein S19P family.
Mass spectrometry	Molecular mass is 10299.6 Da from positions 2 - 92. Determined by MALDI. Ref.8

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: InterPro
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4587209. Source: EcoliWiki
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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.4

Chain

2 – 92

91

30S ribosomal protein S19 HAMAP-Rule MF_00531

PRO_0000129819

Natural variations

Natural variant

83

1

H → Y in MW145; suppresses a rimM deletion.

Experimental info

Sequence conflict

37 – 43

7

RSTIFPN → STIFPDR AA sequence Ref.4

Sequence conflict

86

1

D → N AA sequence Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

92

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Helix

13 – 19

7

Helix

20 – 22

3

Beta strand

23 – 25

3

Beta strand

37 – 39

3

Turn

43 – 46

4

Beta strand

49 – 52

4

Beta strand

54 – 58

5

Beta strand

59 – 61

3

Helix

64 – 66

3

Beta strand

68 – 70

3

Turn

71 – 74

4

Sequences

	Sequence		Length	Mass (Da)
	P0A7U3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 439F951848E95CB8	FASTA	92	10,430
	10 20 30 40 50 60 MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA VHNGRQHVPV 70 80 90 FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 S19 from the small ribosomal subunit of Escherichia coli." Yaguchi M., Wittmann H.G. FEBS Lett. 88:227-230(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-92. Strain: K.
[5]	"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 66-70, CROSS-LINKING TO S13. Strain: K12 / A19.
[6]	"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.
[7]	"The PRC-barrel domain of the ribosome maturation protein RimM mediates binding to ribosomal protein S19 in the 30S ribosomal subunits." Loevgren J.M., Bylund G.O., Srivastava M.K., Lundberg L.A.C., Persson O.P., Wingsle G., Wikstroem P.M. RNA 10:1798-1812(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ABILITY OF VARIANT MW145 TO SUPPRESS A RIMM DELETION. Strain: MW100.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02613 Genomic DNA. Translation: CAA26464.1.
U18997 Genomic DNA. Translation: AAA58113.1.
U00096 Genomic DNA. Translation: AAC76341.1.
AP009048 Genomic DNA. Translation: BAE77975.1.

PIR

R3EC19. F23129.

RefSeq

NP_417775.1. NC_000913.2.
YP_492116.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	S	3-81	[»]
1P6G	electron microscopy	12.30	S	2-92	[»]
1P87	electron microscopy	11.50	S	2-92	[»]
1VS5	X-ray	3.46	S	1-92	[»]
1VS7	X-ray	3.46	S	1-92	[»]
2AVY	X-ray	3.46	S	2-92	[»]
2AW7	X-ray	3.46	S	2-92	[»]
2GY9	electron microscopy	15.00	S	2-87	[»]
2GYB	electron microscopy	15.00	S	2-87	[»]
2I2P	X-ray	3.22	S	2-91	[»]
2I2U	X-ray	3.22	S	2-91	[»]
2QAL	X-ray	3.21	S	2-92	[»]
2QAN	X-ray	3.21	S	2-92	[»]
2QB9	X-ray	3.54	S	2-92	[»]
2QBB	X-ray	3.54	S	2-92	[»]
2QBD	X-ray	3.30	S	2-92	[»]
2QBF	X-ray	3.30	S	2-92	[»]
2QBH	X-ray	4.00	S	2-92	[»]
2QBJ	X-ray	4.00	S	2-92	[»]
2QOU	X-ray	3.93	S	2-92	[»]
2QOW	X-ray	3.93	S	2-92	[»]
2QOY	X-ray	3.50	S	2-92	[»]
2QP0	X-ray	3.50	S	2-92	[»]
2VHO	X-ray	3.74	S	2-92	[»]
2VHP	X-ray	3.74	S	2-92	[»]
2WWL	electron microscopy	5.80	S	3-81	[»]
2YKR	electron microscopy	9.80	S	3-81	[»]
2Z4K	X-ray	4.45	S	2-92	[»]
2Z4M	X-ray	4.45	S	2-92	[»]
3DF1	X-ray	3.50	S	2-91	[»]
3DF3	X-ray	3.50	S	2-91	[»]
3E1A	electron microscopy	-	L	1-92	[»]
3E1C	electron microscopy	-	L	1-92	[»]
3FIH	electron microscopy	6.70	S	3-81	[»]
3I1M	X-ray	3.19	S	1-92	[»]
3I1O	X-ray	3.19	S	1-92	[»]
3I1Q	X-ray	3.81	S	1-92	[»]
3I1S	X-ray	3.81	S	1-92	[»]
3I1Z	X-ray	3.71	S	1-92	[»]
3I21	X-ray	3.71	S	1-92	[»]
3IZV	electron microscopy	-	W	1-92	[»]
3IZW	electron microscopy	-	W	1-92	[»]
3J00	electron microscopy	-	S	2-92	[»]
3J0U	electron microscopy	12.10	V	2-92	[»]
3J0V	electron microscopy	14.70	V	2-92	[»]
3J0X	electron microscopy	13.50	V	2-92	[»]
3J0Z	electron microscopy	11.50	V	2-92	[»]
3J10	electron microscopy	11.50	V	2-92	[»]
3J13	electron microscopy	13.10	U	2-92	[»]
3J18	electron microscopy	8.30	S	3-81	[»]
3KC4	electron microscopy	-	S	1-92	[»]
3OAQ	X-ray	3.25	S	3-81	[»]
3OAR	X-ray	3.25	S	3-81	[»]
3OFA	X-ray	3.19	S	3-81	[»]
3OFB	X-ray	3.19	S	3-81	[»]
3OFO	X-ray	3.10	S	3-81	[»]
3OFP	X-ray	3.10	S	3-81	[»]
3OFX	X-ray	3.29	S	3-81	[»]
3OFY	X-ray	3.29	S	3-81	[»]
3OR9	X-ray	3.30	S	1-92	[»]
3ORA	X-ray	3.30	S	1-92	[»]
3SFS	X-ray	3.20	S	1-92	[»]
3UOQ	X-ray	3.70	S	1-92	[»]
4A2I	electron microscopy	16.50	S	3-81	[»]
4ADV	electron microscopy	13.50	S	2-92	[»]
4GAQ	X-ray	3.30	S	1-92	[»]
4GAS	X-ray	3.30	S	1-92	[»]
4GD1	X-ray	3.00	S	3-81	[»]
4GD2	X-ray	3.00	S	3-81	[»]

ProteinModelPortal

P0A7U3.

SMR

P0A7U3. Positions 2-88.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47904N.

IntAct

P0A7U3. 28 interactions.

STRING

511145.b3316.

Proteomic databases

PaxDb

P0A7U3.

PRIDE

P0A7U3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.

GeneID

12932294.
947811.

KEGG

ecj:Y75_p3860.
eco:b3316.

PATRIC

32122064. VBIEscCol129921_3409.

Organism-specific databases

EchoBASE

EB0911.

EcoGene

EG10918. rpsS.

Phylogenomic databases

eggNOG

COG0185.

HOGENOM

HOG000111560.

KO

K02965.

OMA

RVIKTWS.

ProtClustDB

PRK00357.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Gene expression databases

Genevestigator

P0A7U3.

Family and domain databases

Gene3D

3.30.860.10. 1 hit.

HAMAP

MF_00531. Ribosomal_S19.

InterPro

IPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]

PANTHER

PTHR11880. PTHR11880. 1 hit.

Pfam

PF00203. Ribosomal_S19. 1 hit.
[Graphical view]

PIRSF

PIRSF002144. Ribosomal_S19. 1 hit.

PRINTS

PR00975. RIBOSOMALS19.

SUPFAM

SSF54570. Ribosomal_S19. 1 hit.

TIGRFAMs

TIGR01050. rpsS_bact. 1 hit.

PROSITE

PS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7U3.

Entry information

Entry name

RS19_ECOLI

Accession

Primary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program