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Protein

Starch-binding protein SusD

Gene

susD

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811Glucose
Metal bindingi273 – 2731Calcium
Metal bindingi288 – 2881Calcium; via carbonyl oxygen
Binding sitei296 – 2961Glucose
Binding sitei320 – 3201Glucose
Metal bindingi430 – 4301Calcium; via carbonyl oxygen
Metal bindingi432 – 4321Calcium

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. starch binding Source: UniProtKB

GO - Biological processi

  1. starch catabolic process Source: UniProtKB-UniPathway
  2. starch metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-3767-MONOMER.
UniPathwayiUPA00153.

Protein family/group databases

TCDBi8.A.46.1.1. the glycan-binding protein (susd) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Starch-binding protein SusD
Alternative name(s):
Starch-utilization system protein D
Gene namesi
Name:susD
Ordered Locus Names:BT_3701
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000001414: Chromosome

Subcellular locationi

Cell outer membrane 2 Publications; Lipid-anchor 2 Publications

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-SubCell
  2. outer membrane Source: MENGO
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Abolished ability to grow on amylopectin and pullulan, as well as maltohexaose and maltoheptaose.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424PROSITE-ProRule annotationAdd
BLAST
Chaini25 – 551527Starch-binding protein SusDPRO_0000425883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi25 – 251N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi25 – 251S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Inductioni

By maltose.1 Publication

Interactioni

Subunit structurei

Interacts with SusC.2 Publications

Protein-protein interaction databases

DIPiDIP-46026N.
STRINGi226186.BT_3701.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 413Combined sources
Helixi44 – 5310Combined sources
Turni54 – 563Combined sources
Turni74 – 774Combined sources
Helixi79 – 8810Combined sources
Beta strandi91 – 977Combined sources
Helixi104 – 1096Combined sources
Helixi117 – 13923Combined sources
Turni140 – 1423Combined sources
Helixi146 – 17025Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi185 – 1884Combined sources
Helixi189 – 20315Combined sources
Helixi204 – 2063Combined sources
Turni210 – 2123Combined sources
Helixi220 – 23213Combined sources
Helixi234 – 2385Combined sources
Helixi243 – 25412Combined sources
Helixi264 – 2685Combined sources
Turni270 – 2745Combined sources
Helixi276 – 2794Combined sources
Beta strandi282 – 2865Combined sources
Helixi290 – 2934Combined sources
Helixi294 – 2963Combined sources
Helixi298 – 3047Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi323 – 3253Combined sources
Helixi327 – 3304Combined sources
Turni331 – 3333Combined sources
Helixi337 – 3393Combined sources
Beta strandi351 – 3533Combined sources
Helixi357 – 36610Combined sources
Helixi371 – 3788Combined sources
Helixi404 – 4063Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi433 – 4375Combined sources
Helixi439 – 45113Combined sources
Helixi457 – 46610Combined sources
Helixi478 – 48912Combined sources
Helixi495 – 5017Combined sources
Beta strandi505 – 5073Combined sources
Helixi515 – 5173Combined sources
Helixi526 – 5294Combined sources
Helixi535 – 5406Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ8A1G2.
SMRiQ8A1G2. Positions 37-551.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8A1G2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 753Glucose binding
Regioni98 – 1014Glucose binding

Domaini

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 (PubMed:18611383).1 Publication

Sequence similaritiesi

Belongs to the SusD family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000022810.
OMAiWAGNRCR.
OrthoDBiEOG6K13RW.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR012944. SusD_RagB_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF07980. SusD. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8A1G2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTKYIKQLF SAALIAVLSS GVTSCINDLD ISPIDPQTGG SFDQQGVFVK
60 70 80 90 100
GYAMLGVTGQ KGIDGSPDLD GQDEGESGFY RTTFNCNELP TDECLWAWQE
110 120 130 140 150
NQDIPQLTSI SWSPSSQRTE WVYVRLGYDI TQYNFFLDQT EGMTDAETLR
160 170 180 190 200
QRAEIRFLRA LHYWYFLDLF GKAPFKEHFS NDLPVEKKGT ELYTYIQNEL
210 220 230 240 250
NEIEADMYEP RQAPFGRADK AANWLLRARL YLNAGVYTGQ TDYAKAEEYA
260 270 280 290 300
SKVIGSAYKL CTNYSELFMA DNDENENAMQ EIILPIRQDG VKTRNYGGST
310 320 330 340 350
YLVCGTRVAG MPRMGTTNGW SCIFARAAMV QKFFSNLEDV PMLPADVEIP
360 370 380 390 400
TKGLDTDEQI DAFDAEHGIR TEDMIKAAGD DRALLYSGVG GGRRKIQTDA
410 420 430 440 450
ISGFTDGLSI VKWQNYRSDG KPVSHATYPD TDIPLFRLAE AYLTRAEAIF
460 470 480 490 500
RQGGDATGDI NELRKRANCT RKVQTVTEQE LIDEWAREFY LEGRRRSDLV
510 520 530 540 550
RFGMFTTNKY LWDWKGGAMN GTSVASYYNK YPIPVSDINN NRNMSQNEGY

K
Length:551
Mass (Da):62,309
Last modified:June 1, 2003 - v1
Checksum:iEBBB322E687A5E7F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti423 – 4231V → A in AAB42172. (PubMed:9006015)Curated
Sequence conflicti481 – 4822LI → TNR in AAB42172. (PubMed:9006015)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77614 Genomic DNA. Translation: AAB42172.1. Frameshift.
AE015928 Genomic DNA. Translation: AAO78806.1.
RefSeqiNP_812612.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO78806; AAO78806; BT_3701.
GeneIDi1072099.
KEGGibth:BT_3701.
PATRICi21062403. VBIBacThe70966_3761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77614 Genomic DNA. Translation: AAB42172.1. Frameshift.
AE015928 Genomic DNA. Translation: AAO78806.1.
RefSeqiNP_812612.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ8A1G2.
SMRiQ8A1G2. Positions 37-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46026N.
STRINGi226186.BT_3701.

Protein family/group databases

TCDBi8.A.46.1.1. the glycan-binding protein (susd) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO78806; AAO78806; BT_3701.
GeneIDi1072099.
KEGGibth:BT_3701.
PATRICi21062403. VBIBacThe70966_3761.

Phylogenomic databases

HOGENOMiHOG000022810.
OMAiWAGNRCR.
OrthoDBiEOG6K13RW.

Enzyme and pathway databases

UniPathwayiUPA00153.
BioCyciBTHE226186:GJXV-3767-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8A1G2.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR012944. SusD_RagB_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF07980. SusD. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSUSD_BACTN
AccessioniPrimary (citable) accession number: Q8A1G2
Secondary accession number(s): Q45770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 73 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.