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Q8A1G2

- SUSD_BACTN

UniProt

Q8A1G2 - SUSD_BACTN

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDENENAM.
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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L77614 Genomic DNA. Translation: AAB42172.1 . Frameshift.
AE015928 Genomic DNA. Translation: AAO78806.1 .
RefSeqi NP_812612.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CK7 X-ray 2.10 A/B/C/D 26-551 [» ]
3CK8 X-ray 2.10 A/B 26-551 [» ]
3CK9 X-ray 2.20 A/B 26-551 [» ]
3CKB X-ray 2.30 A/B 26-551 [» ]
3CKC X-ray 1.50 A/B 26-551 [» ]
ProteinModelPortali Q8A1G2.
SMRi Q8A1G2. Positions 37-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-46026N.
STRINGi 226186.BT_3701.

Protein family/group databases

TCDBi 8.A.46.1.1. the glycan-binding protein (susd) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO78806 ; AAO78806 ; BT_3701 .
GeneIDi 1072099.
KEGGi bth:BT_3701.
PATRICi 21062403. VBIBacThe70966_3761.

Phylogenomic databases

HOGENOMi HOG000022810.
OMAi DENENAM.
OrthoDBi EOG6K13RW.

Enzyme and pathway databases

UniPathwayi UPA00153 .
BioCyci BTHE226186:GJXV-3767-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q8A1G2.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR012944. SusD_RagB_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF07980. SusD. 1 hit.
[Graphical view ]
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 71 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