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Q8A1G2

- SUSD_BACTN

UniProt

Q8A1G2 - SUSD_BACTN

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
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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

    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

    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.
    [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

    MKTKYIKQLF SAALIAVLSS GVTSCINDLD ISPIDPQTGG SFDQQGVFVK    50
    GYAMLGVTGQ KGIDGSPDLD GQDEGESGFY RTTFNCNELP TDECLWAWQE 100
    NQDIPQLTSI SWSPSSQRTE WVYVRLGYDI TQYNFFLDQT EGMTDAETLR 150
    QRAEIRFLRA LHYWYFLDLF GKAPFKEHFS NDLPVEKKGT ELYTYIQNEL 200
    NEIEADMYEP RQAPFGRADK AANWLLRARL YLNAGVYTGQ TDYAKAEEYA 250
    SKVIGSAYKL CTNYSELFMA DNDENENAMQ EIILPIRQDG VKTRNYGGST 300
    YLVCGTRVAG MPRMGTTNGW SCIFARAAMV QKFFSNLEDV PMLPADVEIP 350
    TKGLDTDEQI DAFDAEHGIR TEDMIKAAGD DRALLYSGVG GGRRKIQTDA 400
    ISGFTDGLSI VKWQNYRSDG KPVSHATYPD TDIPLFRLAE AYLTRAEAIF 450
    RQGGDATGDI NELRKRANCT RKVQTVTEQE LIDEWAREFY LEGRRRSDLV 500
    RFGMFTTNKY LWDWKGGAMN GTSVASYYNK YPIPVSDINN NRNMSQNEGY 550
    K 551
    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.
    [Graphical view ]
    Pfami PF07980. SusD. 1 hit.
    [Graphical view ]
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 1, 2014
    This is version 70 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