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Protein

Sulfate-binding protein

Gene

sbp

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

Functioni

This protein specifically binds sulfate and is involved in its transmembrane transport.

GO - Molecular functioni

GO - Biological processi

  • sulfur compound metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Sulfate transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:SBP-MONOMER.
ECOL316407:JW3888-MONOMER.
MetaCyc:SBP-MONOMER.
RETL1328306-WGS:GSTH-6118-MONOMER.

Protein family/group databases

TCDBi3.A.1.6.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate-binding protein
Alternative name(s):
Sulfate starvation-induced protein 2
Short name:
SSI2
Gene namesi
Name:sbp
Ordered Locus Names:b3917, JW3888
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10929. sbp.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 329310Sulfate-binding proteinPRO_0000031683Add
BLAST

Proteomic databases

PaxDbiP0AG78.

2D gel databases

SWISS-2DPAGEP0AG78.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Protein-protein interaction databases

BioGridi4261220. 7 interactions.
DIPiDIP-35843N.
IntActiP0AG78. 11 interactions.
STRINGi511145.b3917.

Structurei

3D structure databases

ProteinModelPortaliP0AG78.
SMRiP0AG78. Positions 20-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105DE7. Bacteria.
COG1613. LUCA.
HOGENOMiHOG000260057.
InParanoidiP0AG78.
KOiK02048.
OMAiTIDKDFG.
OrthoDBiEOG6PGK2K.
PhylomeDBiP0AG78.

Family and domain databases

InterProiIPR000957. Sulphate/thiosulphate-bd_CS.
IPR005669. Thiosulph/SO4-bd.
[Graphical view]
PANTHERiPTHR30368. PTHR30368. 1 hit.
TIGRFAMsiTIGR00971. 3a0106s03. 1 hit.
PROSITEiPS00401. PROK_SULFATE_BIND_1. 1 hit.
PS00757. PROK_SULFATE_BIND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AG78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKWGVGLTF LLAATSVMAK DIQLLNVSYD PTRELYEQYN KAFSAHWKQQ
60 70 80 90 100
TGDNVVIRQS HGGSGKQATS VINGIEADVV TLALAYDVDA IAERGRIDKE
110 120 130 140 150
WIKRLPDNSA PYTSTIVFLV RKGNPKQIHD WNDLIKPGVS VITPNPKSSG
160 170 180 190 200
GARWNYLAAW GYALHHNNND QAKAQDFVRA LYKNVEVLDS GARGSTNTFV
210 220 230 240 250
ERGIGDVLIA WENEALLAAN ELGKDKFEIV TPSESILAEP TVSVVDKVVE
260 270 280 290 300
KKGTKEVAEA YLKYLYSPEG QEIAAKNYYR PRDAEVAKKY ENAFPKLKLF
310 320
TIDEEFGGWT KAQKEHFANG GTFDQISKR
Length:329
Mass (Da):36,659
Last modified:December 20, 2005 - v1
Checksum:i3353D36DE484C814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851V → E in CAA26357 (PubMed:3158524).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02519 Genomic DNA. Translation: CAA26357.1. Sequence problems.
L19201 Genomic DNA. Translation: AAB03049.1.
U00096 Genomic DNA. Translation: AAC76899.1.
AP009048 Genomic DNA. Translation: BAE77393.1.
PIRiS40860. BYEC.
RefSeqiNP_418352.1. NC_000913.3.
WP_001045689.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76899; AAC76899; b3917.
BAE77393; BAE77393; BAE77393.
GeneIDi948411.
KEGGiecj:JW3888.
eco:b3917.
PATRICi32123347. VBIEscCol129921_4034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02519 Genomic DNA. Translation: CAA26357.1. Sequence problems.
L19201 Genomic DNA. Translation: AAB03049.1.
U00096 Genomic DNA. Translation: AAC76899.1.
AP009048 Genomic DNA. Translation: BAE77393.1.
PIRiS40860. BYEC.
RefSeqiNP_418352.1. NC_000913.3.
WP_001045689.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AG78.
SMRiP0AG78. Positions 20-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261220. 7 interactions.
DIPiDIP-35843N.
IntActiP0AG78. 11 interactions.
STRINGi511145.b3917.

Protein family/group databases

TCDBi3.A.1.6.1. the atp-binding cassette (abc) superfamily.

2D gel databases

SWISS-2DPAGEP0AG78.

Proteomic databases

PaxDbiP0AG78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76899; AAC76899; b3917.
BAE77393; BAE77393; BAE77393.
GeneIDi948411.
KEGGiecj:JW3888.
eco:b3917.
PATRICi32123347. VBIEscCol129921_4034.

Organism-specific databases

EchoBASEiEB0922.
EcoGeneiEG10929. sbp.

Phylogenomic databases

eggNOGiENOG4105DE7. Bacteria.
COG1613. LUCA.
HOGENOMiHOG000260057.
InParanoidiP0AG78.
KOiK02048.
OMAiTIDKDFG.
OrthoDBiEOG6PGK2K.
PhylomeDBiP0AG78.

Enzyme and pathway databases

BioCyciEcoCyc:SBP-MONOMER.
ECOL316407:JW3888-MONOMER.
MetaCyc:SBP-MONOMER.
RETL1328306-WGS:GSTH-6118-MONOMER.

Miscellaneous databases

PROiP0AG78.

Family and domain databases

InterProiIPR000957. Sulphate/thiosulphate-bd_CS.
IPR005669. Thiosulph/SO4-bd.
[Graphical view]
PANTHERiPTHR30368. PTHR30368. 1 hit.
TIGRFAMsiTIGR00971. 3a0106s03. 1 hit.
PROSITEiPS00401. PROK_SULFATE_BIND_1. 1 hit.
PS00757. PROK_SULFATE_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase."
    Hellinga H.W., Evans P.R.
    Eur. J. Biochem. 149:363-373(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Evans P.R.
    Submitted (OCT-1986) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Engineered interdomain disulfide in the periplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies."
    Jacobson B.L., He J.J., Vermersch P.S., Lemon D.D., Quiocho F.A.
    J. Biol. Chem. 266:5220-5225(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 152-164; 176-178 AND 201-203, MUTAGENESIS.
  4. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "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 20-31.
    Strain: K12 / EMG2.
  8. "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli."
    Quadroni M., Staudenmann W., Kertesz M.A., James P.
    Eur. J. Biochem. 239:773-781(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-29; 42-48; 256-263; 265-273 AND 277-282.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiSUBI_ECOLI
AccessioniPrimary (citable) accession number: P0AG78
Secondary accession number(s): P06997, Q2M8L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.