Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S2

Gene

rpsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for ribosomal protein S1 to bind to the 30S subunit.1 Publication

GO - Molecular functioni

  • structural constituent of ribosome Source: GO_Central
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.
MetaCyc:EG10901-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S2
Gene namesi
Name:rpsB
Ordered Locus Names:b0169, JW0164
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10901. rpsB.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001341652 – 24130S ribosomal protein S2Add BLAST240

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei115N6-succinyllysine1 Publication1

Proteomic databases

EPDiP0A7V0.
PaxDbiP0A7V0.
PRIDEiP0A7V0.

2D gel databases

SWISS-2DPAGEP0A7V0.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit, contacts S1. Some nascent polypeptide chains are able to cross-link to this protein in situ.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hslRP0ACG82EBI-543439,EBI-562824

Protein-protein interaction databases

BioGridi852185. 1 interactor.
DIPiDIP-6877N.
IntActiP0A7V0. 206 interactors.
STRINGi511145.b0169.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Helixi34 – 37Combined sources4
Beta strandi38 – 40Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-B6-214[»]
2YKRelectron microscopy9.80B9-226[»]
3J9Yelectron microscopy3.90b1-240[»]
3J9Zelectron microscopy3.60SB2-241[»]
3JA1electron microscopy3.60SB2-241[»]
3JBUelectron microscopy3.64B1-241[»]
3JBVelectron microscopy3.32B1-241[»]
3JCDelectron microscopy3.70b1-241[»]
3JCEelectron microscopy3.20b1-241[»]
3JCJelectron microscopy3.70j1-241[»]
3JCNelectron microscopy4.60d1-241[»]
4A2Ielectron microscopy16.50B9-226[»]
4ADVelectron microscopy13.50B2-241[»]
4ODLX-ray2.92C/D/E/F20-34[»]
4ODMX-ray1.75E/F/G/H/I/J/K/L/M20-34[»]
4ODNX-ray1.60B26-41[»]
4ODPX-ray1.75B20-34[»]
4U1UX-ray2.95AB/CB9-226[»]
4U1VX-ray3.00AB/CB9-226[»]
4U20X-ray2.90AB/CB9-226[»]
4U24X-ray2.90AB/CB9-226[»]
4U25X-ray2.90AB/CB9-226[»]
4U26X-ray2.80AB/CB9-226[»]
4U27X-ray2.80AB/CB9-226[»]
4V48electron microscopy11.50BB2-241[»]
4V4HX-ray3.46AB/CB1-241[»]
4V4QX-ray3.46AB/CB2-241[»]
4V4Velectron microscopy15.00AB6-241[»]
4V4Welectron microscopy15.00AB6-241[»]
4V50X-ray3.22AB/CB2-241[»]
4V52X-ray3.21AB/CB2-241[»]
4V53X-ray3.54AB/CB2-241[»]
4V54X-ray3.30AB/CB2-241[»]
4V55X-ray4.00AB/CB2-241[»]
4V56X-ray3.93AB/CB2-241[»]
4V57X-ray3.50AB/CB2-241[»]
4V5BX-ray3.74BB/DB2-241[»]
4V5Helectron microscopy5.80AB9-226[»]
4V5YX-ray4.45AB/CB2-241[»]
4V64X-ray3.50AB/CB2-241[»]
4V65electron microscopy9.00AB1-241[»]
4V66electron microscopy9.00AB1-241[»]
4V69electron microscopy6.70AB9-226[»]
4V6CX-ray3.19AB/CB1-241[»]
4V6DX-ray3.81AB/CB1-241[»]
4V6EX-ray3.71AB/CB1-241[»]
4V6Kelectron microscopy8.25BF1-241[»]
4V6Lelectron microscopy13.20AF1-241[»]
4V6Melectron microscopy7.10AB2-241[»]
4V6Nelectron microscopy12.10BE2-241[»]
4V6Oelectron microscopy14.70AE2-241[»]
4V6Pelectron microscopy13.50AE2-241[»]
4V6Qelectron microscopy11.50AE2-241[»]
4V6Relectron microscopy11.50AE2-241[»]
4V6Selectron microscopy13.10BD2-241[»]
4V6Telectron microscopy8.30AB9-226[»]
4V6Velectron microscopy9.80AB2-241[»]
4V6Yelectron microscopy12.00AB9-226[»]
4V6Zelectron microscopy12.00AB9-226[»]
4V70electron microscopy17.00AB9-226[»]
4V71electron microscopy20.00AB9-226[»]
4V72electron microscopy13.00AB9-226[»]
4V73electron microscopy15.00AB9-226[»]
4V74electron microscopy17.00AB9-226[»]
4V75electron microscopy12.00AB9-226[»]
4V76electron microscopy17.00AB9-226[»]
4V77electron microscopy17.00AB9-226[»]
4V78electron microscopy20.00AB9-226[»]
4V79electron microscopy15.00AB9-226[»]
4V7Aelectron microscopy9.00AB9-226[»]
4V7Belectron microscopy6.80AB1-241[»]
4V7Celectron microscopy7.60AB2-241[»]
4V7Delectron microscopy7.60BB2-241[»]
4V7Ielectron microscopy9.60BB1-241[»]
4V7SX-ray3.25AB/CB9-226[»]
4V7TX-ray3.19AB/CB9-226[»]
4V7UX-ray3.10AB/CB9-226[»]
4V7VX-ray3.29AB/CB9-226[»]
4V85X-ray3.20B1-241[»]
4V89X-ray3.70AB1-241[»]
4V9CX-ray3.30AB/CB1-241[»]
4V9DX-ray3.00AB/BB9-226[»]
4V9OX-ray2.90BB/DB/FB/HB1-241[»]
4V9PX-ray2.90BB/DB/FB/HB1-241[»]
4WF1X-ray3.09AB/CB9-226[»]
4WOIX-ray3.00AB/DB1-241[»]
4WWWX-ray3.10QB/XB9-226[»]
4YBBX-ray2.10AB/BB4-227[»]
5AFIelectron microscopy2.90b1-240[»]
5IQRelectron microscopy3.00g1-241[»]
5IT8X-ray3.12AB/BB4-227[»]
5J5BX-ray2.80AB/BB4-227[»]
5J7LX-ray3.00AB/BB4-227[»]
5J88X-ray3.32AB/BB4-227[»]
5J8AX-ray3.10AB/BB4-227[»]
5J91X-ray2.96AB/BB4-227[»]
5JC9X-ray3.03AB/BB4-227[»]
5JTEelectron microscopy3.60AB1-240[»]
5JU8electron microscopy3.60AB1-240[»]
5KCRelectron microscopy3.601b1-241[»]
5KCSelectron microscopy3.901b1-241[»]
5KPSelectron microscopy3.9071-241[»]
5KPVelectron microscopy4.1061-241[»]
5KPWelectron microscopy3.9061-241[»]
5KPXelectron microscopy3.9061-241[»]
5L3Pelectron microscopy3.70b1-240[»]
ProteinModelPortaliP0A7V0.
SMRiP0A7V0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.Curated

Phylogenomic databases

eggNOGiENOG4105CE9. Bacteria.
COG0052. LUCA.
HOGENOMiHOG000071892.
InParanoidiP0A7V0.
KOiK02967.
OMAiRIPDILY.
PhylomeDBiP0A7V0.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_00291_B. Ribosomal_S2_B. 1 hit.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7V0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVSMRDML KAGVHFGHQT RYWNPKMKPF IFGARNKVHI INLEKTVPMF
60 70 80 90 100
NEALAELNKI ASRKGKILFV GTKRAASEAV KDAALSCDQF FVNHRWLGGM
110 120 130 140 150
LTNWKTVRQS IKRLKDLETQ SQDGTFDKLT KKEALMRTRE LEKLENSLGG
160 170 180 190 200
IKDMGGLPDA LFVIDADHEH IAIKEANNLG IPVFAIVDTN SDPDGVDFVI
210 220 230 240
PGNDDAIRAV TLYLGAVAAT VREGRSQDLA SQAEESFVEA E
Length:241
Mass (Da):26,744
Last modified:January 23, 2007 - v2
Checksum:i87A38C696115212E
GO

Mass spectrometryi

Molecular mass is 26610.5 Da from positions 2 - 241. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.
PIRiA02696. R3EC2.
RefSeqiNP_414711.1. NC_000913.3.
WP_000246882.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.
GeneIDi947874.
KEGGiecj:JW0164.
eco:b0169.
PATRICi32115445. VBIEscCol129921_0174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.
PIRiA02696. R3EC2.
RefSeqiNP_414711.1. NC_000913.3.
WP_000246882.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-B6-214[»]
2YKRelectron microscopy9.80B9-226[»]
3J9Yelectron microscopy3.90b1-240[»]
3J9Zelectron microscopy3.60SB2-241[»]
3JA1electron microscopy3.60SB2-241[»]
3JBUelectron microscopy3.64B1-241[»]
3JBVelectron microscopy3.32B1-241[»]
3JCDelectron microscopy3.70b1-241[»]
3JCEelectron microscopy3.20b1-241[»]
3JCJelectron microscopy3.70j1-241[»]
3JCNelectron microscopy4.60d1-241[»]
4A2Ielectron microscopy16.50B9-226[»]
4ADVelectron microscopy13.50B2-241[»]
4ODLX-ray2.92C/D/E/F20-34[»]
4ODMX-ray1.75E/F/G/H/I/J/K/L/M20-34[»]
4ODNX-ray1.60B26-41[»]
4ODPX-ray1.75B20-34[»]
4U1UX-ray2.95AB/CB9-226[»]
4U1VX-ray3.00AB/CB9-226[»]
4U20X-ray2.90AB/CB9-226[»]
4U24X-ray2.90AB/CB9-226[»]
4U25X-ray2.90AB/CB9-226[»]
4U26X-ray2.80AB/CB9-226[»]
4U27X-ray2.80AB/CB9-226[»]
4V48electron microscopy11.50BB2-241[»]
4V4HX-ray3.46AB/CB1-241[»]
4V4QX-ray3.46AB/CB2-241[»]
4V4Velectron microscopy15.00AB6-241[»]
4V4Welectron microscopy15.00AB6-241[»]
4V50X-ray3.22AB/CB2-241[»]
4V52X-ray3.21AB/CB2-241[»]
4V53X-ray3.54AB/CB2-241[»]
4V54X-ray3.30AB/CB2-241[»]
4V55X-ray4.00AB/CB2-241[»]
4V56X-ray3.93AB/CB2-241[»]
4V57X-ray3.50AB/CB2-241[»]
4V5BX-ray3.74BB/DB2-241[»]
4V5Helectron microscopy5.80AB9-226[»]
4V5YX-ray4.45AB/CB2-241[»]
4V64X-ray3.50AB/CB2-241[»]
4V65electron microscopy9.00AB1-241[»]
4V66electron microscopy9.00AB1-241[»]
4V69electron microscopy6.70AB9-226[»]
4V6CX-ray3.19AB/CB1-241[»]
4V6DX-ray3.81AB/CB1-241[»]
4V6EX-ray3.71AB/CB1-241[»]
4V6Kelectron microscopy8.25BF1-241[»]
4V6Lelectron microscopy13.20AF1-241[»]
4V6Melectron microscopy7.10AB2-241[»]
4V6Nelectron microscopy12.10BE2-241[»]
4V6Oelectron microscopy14.70AE2-241[»]
4V6Pelectron microscopy13.50AE2-241[»]
4V6Qelectron microscopy11.50AE2-241[»]
4V6Relectron microscopy11.50AE2-241[»]
4V6Selectron microscopy13.10BD2-241[»]
4V6Telectron microscopy8.30AB9-226[»]
4V6Velectron microscopy9.80AB2-241[»]
4V6Yelectron microscopy12.00AB9-226[»]
4V6Zelectron microscopy12.00AB9-226[»]
4V70electron microscopy17.00AB9-226[»]
4V71electron microscopy20.00AB9-226[»]
4V72electron microscopy13.00AB9-226[»]
4V73electron microscopy15.00AB9-226[»]
4V74electron microscopy17.00AB9-226[»]
4V75electron microscopy12.00AB9-226[»]
4V76electron microscopy17.00AB9-226[»]
4V77electron microscopy17.00AB9-226[»]
4V78electron microscopy20.00AB9-226[»]
4V79electron microscopy15.00AB9-226[»]
4V7Aelectron microscopy9.00AB9-226[»]
4V7Belectron microscopy6.80AB1-241[»]
4V7Celectron microscopy7.60AB2-241[»]
4V7Delectron microscopy7.60BB2-241[»]
4V7Ielectron microscopy9.60BB1-241[»]
4V7SX-ray3.25AB/CB9-226[»]
4V7TX-ray3.19AB/CB9-226[»]
4V7UX-ray3.10AB/CB9-226[»]
4V7VX-ray3.29AB/CB9-226[»]
4V85X-ray3.20B1-241[»]
4V89X-ray3.70AB1-241[»]
4V9CX-ray3.30AB/CB1-241[»]
4V9DX-ray3.00AB/BB9-226[»]
4V9OX-ray2.90BB/DB/FB/HB1-241[»]
4V9PX-ray2.90BB/DB/FB/HB1-241[»]
4WF1X-ray3.09AB/CB9-226[»]
4WOIX-ray3.00AB/DB1-241[»]
4WWWX-ray3.10QB/XB9-226[»]
4YBBX-ray2.10AB/BB4-227[»]
5AFIelectron microscopy2.90b1-240[»]
5IQRelectron microscopy3.00g1-241[»]
5IT8X-ray3.12AB/BB4-227[»]
5J5BX-ray2.80AB/BB4-227[»]
5J7LX-ray3.00AB/BB4-227[»]
5J88X-ray3.32AB/BB4-227[»]
5J8AX-ray3.10AB/BB4-227[»]
5J91X-ray2.96AB/BB4-227[»]
5JC9X-ray3.03AB/BB4-227[»]
5JTEelectron microscopy3.60AB1-240[»]
5JU8electron microscopy3.60AB1-240[»]
5KCRelectron microscopy3.601b1-241[»]
5KCSelectron microscopy3.901b1-241[»]
5KPSelectron microscopy3.9071-241[»]
5KPVelectron microscopy4.1061-241[»]
5KPWelectron microscopy3.9061-241[»]
5KPXelectron microscopy3.9061-241[»]
5L3Pelectron microscopy3.70b1-240[»]
ProteinModelPortaliP0A7V0.
SMRiP0A7V0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852185. 1 interactor.
DIPiDIP-6877N.
IntActiP0A7V0. 206 interactors.
STRINGi511145.b0169.

2D gel databases

SWISS-2DPAGEP0A7V0.

Proteomic databases

EPDiP0A7V0.
PaxDbiP0A7V0.
PRIDEiP0A7V0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.
GeneIDi947874.
KEGGiecj:JW0164.
eco:b0169.
PATRICi32115445. VBIEscCol129921_0174.

Organism-specific databases

EchoBASEiEB0894.
EcoGeneiEG10901. rpsB.

Phylogenomic databases

eggNOGiENOG4105CE9. Bacteria.
COG0052. LUCA.
HOGENOMiHOG000071892.
InParanoidiP0A7V0.
KOiK02967.
OMAiRIPDILY.
PhylomeDBiP0A7V0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.
MetaCyc:EG10901-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7V0.
PROiP0A7V0.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_00291_B. Ribosomal_S2_B. 1 hit.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS2_ECOLI
AccessioniPrimary (citable) accession number: P0A7V0
Secondary accession number(s): P02351, Q9R2E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.