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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: starch degradation

This protein is involved in the pathway starch degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway starch degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81Glucose1
Metal bindingi273Calcium1
Metal bindingi288Calcium; via carbonyl oxygen1
Binding sitei296Glucose1
Binding sitei320Glucose1
Metal bindingi430Calcium; via carbonyl oxygen1
Metal bindingi432Calcium1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • starch binding Source: UniProtKB

GO - Biological processi

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

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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
Proteomesi
  • UP000001414 Componenti: Chromosome

Subcellular locationi

  • Cell outer membrane 2 Publications; Lipid-anchor 2 Publications

GO - Cellular componenti

  • cell outer membrane Source: UniProtKB-SubCell
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24PROSITE-ProRule annotationAdd BLAST24
ChainiPRO_000042588325 – 551Starch-binding protein SusDAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi25N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi25S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ8A1G2.

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

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 41Combined sources3
Helixi44 – 53Combined sources10
Turni54 – 56Combined sources3
Turni61 – 63Combined sources3
Beta strandi64 – 66Combined sources3
Turni74 – 77Combined sources4
Helixi79 – 88Combined sources10
Beta strandi91 – 97Combined sources7
Helixi104 – 109Combined sources6
Helixi117 – 139Combined sources23
Turni140 – 142Combined sources3
Helixi146 – 170Combined sources25
Beta strandi171 – 175Combined sources5
Beta strandi180 – 182Combined sources3
Beta strandi185 – 188Combined sources4
Helixi189 – 203Combined sources15
Helixi204 – 206Combined sources3
Turni210 – 212Combined sources3
Helixi220 – 232Combined sources13
Helixi234 – 238Combined sources5
Helixi243 – 254Combined sources12
Helixi264 – 268Combined sources5
Turni270 – 274Combined sources5
Helixi276 – 279Combined sources4
Beta strandi282 – 286Combined sources5
Helixi290 – 293Combined sources4
Helixi294 – 296Combined sources3
Helixi298 – 304Combined sources7
Beta strandi315 – 317Combined sources3
Beta strandi323 – 325Combined sources3
Helixi327 – 330Combined sources4
Turni331 – 333Combined sources3
Helixi337 – 339Combined sources3
Beta strandi351 – 353Combined sources3
Helixi357 – 366Combined sources10
Helixi371 – 378Combined sources8
Helixi404 – 406Combined sources3
Beta strandi426 – 428Combined sources3
Beta strandi433 – 437Combined sources5
Helixi439 – 451Combined sources13
Helixi457 – 466Combined sources10
Helixi478 – 489Combined sources12
Helixi495 – 501Combined sources7
Beta strandi505 – 507Combined sources3
Helixi515 – 517Combined sources3
Helixi526 – 529Combined sources4
Helixi535 – 540Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8A1G2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 75Glucose binding3
Regioni98 – 101Glucose binding4

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.
OMAiMGDNGEN.
OrthoDBiPOG091H0IZU.

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]
SUPFAMiSSF48452. SSF48452. 1 hit.
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 differs from that shown. Reason: Frameshift at positions 436, 461, 465, 467, 475 and 476.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti423V → A in AAB42172 (PubMed:9006015).Curated1
Sequence conflicti481 – 482LI → TNR in AAB42172 (PubMed:9006015).Curated2

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.
WP_008767005.1. 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.
WP_008767005.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.

Proteomic databases

PaxDbiQ8A1G2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000022810.
OMAiMGDNGEN.
OrthoDBiPOG091H0IZU.

Enzyme and pathway databases

UniPathwayiUPA00153.

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]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 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

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

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.