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Q8A1G2 (SUSD_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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:
Starch-binding protein SusD
Alternative name(s):
Starch-utilization system protein D
Gene names
Name:susD
Ordered Locus Names:BT_3701
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. Ref.1 Ref.3 Ref.4 Ref.5

Pathway

Glycan degradation; starch degradation.

Subunit structure

Interacts with SusC. Ref.4 Ref.5

Subcellular location

Cell outer membrane; Lipid-anchor Probable Ref.1 Ref.3.

Induction

By maltose. Ref.1

Domain

The binding pocket contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Binds cyclic oligosaccharides with higher affinity than linear forms (Ref.5).

Disruption phenotype

Abolished ability to grow on amylopectin and pullulan, as well as maltohexaose and maltoheptaose. Ref.5

Sequence similarities

Belongs to the SusD family.

Sequence caution

The sequence AAB42172.1 differs from that shown. Reason: Frameshift at positions 436, 461, 465, 467, 475 and 476.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCell outer membrane
Membrane
   DomainSignal
   LigandCalcium
Metal-binding
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentouter membrane

Inferred from direct assay Ref.1. Source: MENGO

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from direct assay Ref.1. Source: MENGO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 551527Starch-binding protein SusD
PRO_0000425883

Regions

Region73 – 753Glucose binding
Region98 – 1014Glucose binding

Sites

Metal binding2731Calcium
Metal binding2881Calcium; via carbonyl oxygen
Metal binding4301Calcium; via carbonyl oxygen
Metal binding4321Calcium
Binding site811Glucose
Binding site2961Glucose
Binding site3201Glucose

Amino acid modifications

Lipidation251N-palmitoyl cysteine Potential
Lipidation251S-diacylglycerol cysteine Potential

Experimental info

Sequence conflict4231V → A in AAB42172. Ref.1
Sequence conflict481 – 4822LI → TNR in AAB42172. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8A1G2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EBBB322E687A5E7F

FASTA55162,309
        10         20         30         40         50         60 
MKTKYIKQLF SAALIAVLSS GVTSCINDLD ISPIDPQTGG SFDQQGVFVK GYAMLGVTGQ 

        70         80         90        100        110        120 
KGIDGSPDLD GQDEGESGFY RTTFNCNELP TDECLWAWQE NQDIPQLTSI SWSPSSQRTE 

       130        140        150        160        170        180 
WVYVRLGYDI TQYNFFLDQT EGMTDAETLR QRAEIRFLRA LHYWYFLDLF GKAPFKEHFS 

       190        200        210        220        230        240 
NDLPVEKKGT ELYTYIQNEL NEIEADMYEP RQAPFGRADK AANWLLRARL YLNAGVYTGQ 

       250        260        270        280        290        300 
TDYAKAEEYA SKVIGSAYKL CTNYSELFMA DNDENENAMQ EIILPIRQDG VKTRNYGGST 

       310        320        330        340        350        360 
YLVCGTRVAG MPRMGTTNGW SCIFARAAMV QKFFSNLEDV PMLPADVEIP TKGLDTDEQI 

       370        380        390        400        410        420 
DAFDAEHGIR TEDMIKAAGD DRALLYSGVG GGRRKIQTDA ISGFTDGLSI VKWQNYRSDG 

       430        440        450        460        470        480 
KPVSHATYPD TDIPLFRLAE AYLTRAEAIF RQGGDATGDI NELRKRANCT RKVQTVTEQE 

       490        500        510        520        530        540 
LIDEWAREFY LEGRRRSDLV RFGMFTTNKY LWDWKGGAMN GTSVASYYNK YPIPVSDINN 

       550 
NRNMSQNEGY K 

« 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, FUNCTION, SUBCELLULAR LOCATION.
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]"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, SUBCELLULAR LOCATION.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[4]"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 SUSC.
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[5]"Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices."
Koropatkin N.M., Martens E.C., Gordon J.I., Smith T.J.
Structure 16:1105-1115(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 26-551 IN COMPLEXES WITH CALCIUM AND MALTOHEPTAOSE, FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77614 Genomic DNA. Translation: AAB42172.1. Frameshift.
AE015928 Genomic DNA. Translation: AAO78806.1.
RefSeqNP_812612.1. NC_004663.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CK7X-ray2.10A/B/C/D26-551[»]
3CK8X-ray2.10A/B26-551[»]
3CK9X-ray2.20A/B26-551[»]
3CKBX-ray2.30A/B26-551[»]
3CKCX-ray1.50A/B26-551[»]
ProteinModelPortalQ8A1G2.
SMRQ8A1G2. Positions 37-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46026N.
STRING226186.BT_3701.

Protein family/group databases

TCDB8.A.46.1.1. the glycan-binding protein (susd) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78806; AAO78806; BT_3701.
GeneID1072099.
KEGGbth:BT_3701.
PATRIC21062403. VBIBacThe70966_3761.

Phylogenomic databases

HOGENOMHOG000022810.
OMADENENAM.
OrthoDBEOG6K13RW.
ProtClustDBCLSK823607.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3767-MONOMER.
UniPathwayUPA00153.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR012944. SusD_RagB_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF07980. SusD. 1 hit.
[Graphical view]
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8A1G2.

Entry information

Entry nameSUSD_BACTN
AccessionPrimary (citable) accession number: Q8A1G2
Secondary accession number(s): Q45770
Entry history
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 67 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