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Protein

30S ribosomal protein S2

Gene

rpsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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: CAFA
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER
MetaCyc:EG10901-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S2
Alternative name(s):
Small ribosomal subunit protein uS21 Publication
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

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-2DPAGEiP0A7V0

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit, contacts S1 (PubMed:12068815). Some nascent polypeptide chains are able to cross-link to this protein in situ (PubMed:9716382).12 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4260812, 49 interactors
852185, 1 interactor
DIPiDIP-6877N
IntActiP0A7V0, 208 interactors
STRINGi316385.ECDH10B_0149

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A7V0
SMRiP0A7V0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V0

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CE9 Bacteria
COG0052 LUCA
HOGENOMiHOG000071892
InParanoidiP0A7V0
KOiK02967
PhylomeDBiP0A7V0

Family and domain databases

CDDicd01425 RPS2, 1 hit
HAMAPiMF_00291_B Ribosomal_S2_B, 1 hit
InterProiView protein in InterPro
IPR001865 Ribosomal_S2
IPR005706 Ribosomal_S2_bac/mit/plastid
IPR018130 Ribosomal_S2_CS
IPR023591 Ribosomal_S2_flav_dom_sf
PANTHERiPTHR12534 PTHR12534, 1 hit
PfamiView protein in Pfam
PF00318 Ribosomal_S2, 1 hit
PRINTSiPR00395 RIBOSOMALS2
SUPFAMiSSF52313 SSF52313, 1 hit
TIGRFAMsiTIGR01011 rpsB_bact, 1 hit
PROSITEiView protein in PROSITE
PS00962 RIBOSOMAL_S2_1, 1 hit
PS00963 RIBOSOMAL_S2_2, 1 hit

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
PATRICifig|1411691.4.peg.2112

Similar proteinsi

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[»]
5H5Uelectron microscopy3.00i2-241[»]
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[»]
5LZAelectron microscopy3.60b9-226[»]
5LZBelectron microscopy5.30b9-226[»]
5LZCelectron microscopy4.80b9-226[»]
5LZDelectron microscopy3.40b9-226[»]
5LZEelectron microscopy3.50b9-226[»]
5LZFelectron microscopy4.60b9-226[»]
5MDVelectron microscopy2.97g1-241[»]
5MDWelectron microscopy3.06g1-241[»]
5MDYelectron microscopy3.35g1-241[»]
5MDZelectron microscopy3.10g1-241[»]
5ME0electron microscopy13.50B1-241[»]
5ME1electron microscopy13.50B1-241[»]
5MGPelectron microscopy3.10b9-226[»]
5MY1electron microscopy7.60B2-241[»]
5NO3electron microscopy5.16B4-227[»]
5NP6electron microscopy3.60E9-226[»]
5NWYelectron microscopy2.9319-241[»]
5O2Relectron microscopy3.40b9-226[»]
5U4Ielectron microscopy3.50b1-241[»]
5U9Felectron microscopy3.20B1-241[»]
5U9Gelectron microscopy3.20B1-241[»]
5UYKelectron microscopy3.90B9-226[»]
5UYLelectron microscopy3.60B9-226[»]
5UYMelectron microscopy3.20B9-226[»]
5UYNelectron microscopy4.00B9-226[»]
5UYPelectron microscopy3.90B9-226[»]
5UYQelectron microscopy3.80B9-226[»]
5UZ4electron microscopy5.80B1-241[»]
5WDTelectron microscopy3.00b9-226[»]
5WE4electron microscopy3.10b9-226[»]
5WE6electron microscopy3.40b9-226[»]
5WFKelectron microscopy3.40b9-226[»]
6BU8electron microscopy3.50B2-226[»]
6C4Ielectron microscopy3.24b1-241[»]
6ENFelectron microscopy3.20b9-226[»]
6ENJelectron microscopy3.70b9-226[»]
6ENUelectron microscopy3.10b9-226[»]
6GWTelectron microscopy3.80b9-226[»]
6GXMelectron microscopy3.80b9-226[»]
6GXNelectron microscopy3.90b9-226[»]
6GXOelectron microscopy3.90b9-226[»]
6GXPelectron microscopy4.40b9-226[»]
6H4Nelectron microscopy3.00b9-226[»]
6H58electron microscopy7.90b/bb9-226[»]
ProteinModelPortaliP0A7V0
SMRiP0A7V0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260812, 49 interactors
852185, 1 interactor
DIPiDIP-6877N
IntActiP0A7V0, 208 interactors
STRINGi316385.ECDH10B_0149

2D gel databases

SWISS-2DPAGEiP0A7V0

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
PATRICifig|1411691.4.peg.2112

Organism-specific databases

EchoBASEiEB0894
EcoGeneiEG10901 rpsB

Phylogenomic databases

eggNOGiENOG4105CE9 Bacteria
COG0052 LUCA
HOGENOMiHOG000071892
InParanoidiP0A7V0
KOiK02967
PhylomeDBiP0A7V0

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER
MetaCyc:EG10901-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7V0
PROiPR:P0A7V0

Family and domain databases

CDDicd01425 RPS2, 1 hit
HAMAPiMF_00291_B Ribosomal_S2_B, 1 hit
InterProiView protein in InterPro
IPR001865 Ribosomal_S2
IPR005706 Ribosomal_S2_bac/mit/plastid
IPR018130 Ribosomal_S2_CS
IPR023591 Ribosomal_S2_flav_dom_sf
PANTHERiPTHR12534 PTHR12534, 1 hit
PfamiView protein in Pfam
PF00318 Ribosomal_S2, 1 hit
PRINTSiPR00395 RIBOSOMALS2
SUPFAMiSSF52313 SSF52313, 1 hit
TIGRFAMsiTIGR01011 rpsB_bact, 1 hit
PROSITEiView protein in PROSITE
PS00962 RIBOSOMAL_S2_1, 1 hit
PS00963 RIBOSOMAL_S2_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS2_ECOLI
AccessioniPrimary (citable) accession number: P0A7V0
Secondary accession number(s): P02351, Q9R2E5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 139 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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