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G8JZT0 (SUSE_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer membrane protein SusE
Alternative name(s):
Starch-utilization system protein E
Gene names
Name:susE
Ordered Locus Names:BT_3700
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF. Ref.3 Ref.4 Ref.5

Pathway

Glycan degradation; starch degradation.

Subunit structure

Monomer Probable. Interacts with SusF. Ref.3 Ref.5

Subcellular location

Cell outer membrane; Lipid-anchor Ref.5.

Induction

By maltose. Ref.1

Domain

The carbohydrate binding modules (CBM) mediate starch-binding (Ref.5).

Sequence similarities

Belongs to the SusE family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCell outer membrane
Membrane
   DomainSignal
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processstarch catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

outer membrane

Inferred from direct assay Ref.1. Source: MENGO

   Molecular_functionstarch binding

Inferred from direct assay PubMed 21219452. Source: MENGO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 387367Outer membrane protein SusE
PRO_0000425889

Regions

Region174 – 283110Carbohydrate binding module (CBM) 1
Region284 – 387104Carbohydrate binding module (CBM) 2
Region350 – 3556Glucose binding

Sites

Binding site3261Glucose
Binding site3351Glucose

Amino acid modifications

Lipidation211N-palmitoyl cysteine Probable
Lipidation211S-diacylglycerol cysteine Probable

Experimental info

Mutagenesis211C → A: Abolishes cell outer membrane localization. Ref.5
Mutagenesis1921W → A: Impaired binding to starch; when associated with A-221; A-229 and A-252. Abolished binding to starch; when associated with A-221; A-229; A-252; A-326; A-336 and A-350. Ref.5
Mutagenesis2211K → A: Impaired binding to starch; when associated with A-192; A-229 and A-252. Abolished binding to starch; when associated with A-192; A-229; A-252; A-326; A-336 and A-350. Ref.5
Mutagenesis2291Y → A: Impaired binding to starch; when associated with A-192; A-221 and A-252. Abolished binding to starch; when associated with A-192; A-221; A-252; A-326; A-336 and A-350. Ref.5
Mutagenesis2521N → A: Impaired binding to starch; when associated with A-192; A-221 and A-229. Abolished binding to starch; when associated with A-192; A-221; A-229; A-326; A-336 and A-350. Ref.5
Mutagenesis3261R → A: Impaired binding to starch; when associated with A-336 and A-350. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-336 and A-350. Ref.5
Mutagenesis3361W → A: Impaired binding to starch; when associated with A-326 and A-350. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-326; and A-350. Ref.5
Mutagenesis3501R → A: Impaired binding to starch; when associated with A-326 and A-336. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-326 and A-336. Ref.5

Secondary structure

...................................... 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
G8JZT0 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: D6D0620E02BE6980

FASTA38742,755
        10         20         30         40         50         60 
MKKISNILLA VTFALPLFTA CETDNDSNPI LNEPDTFTLN TPAYAANNVY DLKNAQTVEL 

        70         80         90        100        110        120 
TCSQPDYGFP AATTYTVQAS FEQDFIEATD ESKANYTVLE STSPTAKINV DASELNNALL 

       130        140        150        160        170        180 
DLWTAVNGEQ AELPTEPVAV YIRLKANITS SGKGVCFSNV IELPNVLISK STSSLTPPKT 

       190        200        210        220        230        240 
MFIVGSMLDT DWKVWKPMAG VYGMDGQFYS MIYFDANSEF KFGTKENEYI GINDNRVTVT 

       250        260        270        280        290        300 
DKAGAGVSGS DNFVVENAGW YLFYVKAAVK GDDYQFTITF YPAEVYLFGN TTGGSWAFND 

       310        320        330        340        350        360 
EWKFTVPATK DGNFVSPAMT ASGEVRMCFK TDLDWWRTEF TLHDGEIFYR DFNLIDSWTE 

       370        380 
KGDGYSIQGS AGNVIHLNFT AGTGEKK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of four outer membrane proteins that play a role in utilization of starch by Bacteroides thetaiotaomicron."
Reeves A.R., Wang G.R., Salyers A.A.
J. Bacteriol. 179:643-649(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[2]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[3]"Biochemical analysis of interactions between outer membrane proteins that contribute to starch utilization by Bacteroides thetaiotaomicron."
Cho K.H., Salyers A.A.
J. Bacteriol. 183:7224-7230(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUSF.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[4]"Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron."
Shipman J.A., Berleman J.E., Salyers A.A.
J. Bacteriol. 182:5365-5372(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, STARCH-BINDING.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[5]"Multidomain carbohydrate-binding proteins involved in bacteroides thetaiotaomicron starch metabolism."
Cameron E.A., Maynard M.A., Smith C.J., Smith T.J., Koropatkin N.M., Martens E.C.
J. Biol. Chem. 287:34614-34625(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-387 IN COMPLEX WITH ALPHA-D-GLUCOSE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, STARCH-BINDING, PALMITOYLATION AT CYS-21, MUTAGENESIS OF CYS-21; TRP-192; LYS-221; TYR-229; ASN-252; ARG-326; TRP-336 AND ARG-350.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77615 Genomic DNA. Translation: AAB42171.1.
AE015928 Genomic DNA. Translation: AAO78805.1.
RefSeqNP_812611.1. NC_004663.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FCHX-ray1.30A/B171-387[»]
4FEMX-ray2.50A35-387[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78805; AAO78805; BT_3700.
GeneID1076278.
KEGGbth:BT_3700.

Phylogenomic databases

OMATEHTINI.
OrthoDBEOG6H4K93.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3766-MONOMER.
UniPathwayUPA00153.

Family and domain databases

InterProIPR025970. SusE.
[Graphical view]
PfamPF14292. SusE. 1 hit.
[Graphical view]
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUSE_BACTN
AccessionPrimary (citable) accession number: G8JZT0
Secondary accession number(s): Q45769, Q7C3Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: January 25, 2012
Last modified: May 14, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways