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G8JZT0

- SUSE_BACTN

UniProt

G8JZT0 - SUSE_BACTN

Protein

Outer membrane protein SusE

Gene

susE

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 18 (01 Oct 2014)
      Sequence version 1 (25 Jan 2012)
      Previous versions | rss
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    Functioni

    Starch-binding protein present at the surface of the cell. Mediates starch-binding before starch transport in the periplasm for degradation. SusE and SusF do not constitute the major starch-binding proteins in starch degradation pathway. Has higher affinity for starch compared to SusF.3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei326 – 3261Glucose
    Binding sitei335 – 3351Glucose

    GO - Molecular functioni

    1. starch binding Source: MENGO

    GO - Biological processi

    1. starch catabolic process Source: UniProtKB-UniPathway

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-3766-MONOMER.
    UniPathwayiUPA00153.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Outer membrane protein SusE
    Alternative name(s):
    Starch-utilization system protein E
    Gene namesi
    Name:susE
    Ordered Locus Names:BT_3700
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414: Chromosome

    Subcellular locationi

    Cell outer membrane 1 Publication; Lipid-anchor 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211C → A: Abolishes cell outer membrane localization. 1 Publication
    Mutagenesisi192 – 1921W → A: Impaired binding to starch; when associated with A-221; A-229 and A-252. Abolished binding to starch; when associated with A-221; A-229; A-252; A-326; A-336 and A-350. 1 Publication
    Mutagenesisi221 – 2211K → A: Impaired binding to starch; when associated with A-192; A-229 and A-252. Abolished binding to starch; when associated with A-192; A-229; A-252; A-326; A-336 and A-350. 1 Publication
    Mutagenesisi229 – 2291Y → A: Impaired binding to starch; when associated with A-192; A-221 and A-252. Abolished binding to starch; when associated with A-192; A-221; A-252; A-326; A-336 and A-350. 1 Publication
    Mutagenesisi252 – 2521N → A: Impaired binding to starch; when associated with A-192; A-221 and A-229. Abolished binding to starch; when associated with A-192; A-221; A-229; A-326; A-336 and A-350. 1 Publication
    Mutagenesisi326 – 3261R → A: Impaired binding to starch; when associated with A-336 and A-350. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-336 and A-350. 1 Publication
    Mutagenesisi336 – 3361W → A: Impaired binding to starch; when associated with A-326 and A-350. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-326; and A-350. 1 Publication
    Mutagenesisi350 – 3501R → A: Impaired binding to starch; when associated with A-326 and A-336. Abolished binding to starch; when associated with A-192; A-221; A-229; A-252; A-326 and A-336. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020PROSITE-ProRule annotationAdd
    BLAST
    Chaini21 – 387367Outer membrane protein SusEPRO_0000425889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi21 – 211N-palmitoyl cysteine1 Publication
    Lipidationi21 – 211S-diacylglycerol cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate

    Expressioni

    Inductioni

    By maltose.1 Publication

    Interactioni

    Subunit structurei

    Monomer Probable. Interacts with SusF.2 PublicationsCurated

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi182 – 1854
    Turni186 – 1883
    Beta strandi195 – 1973
    Beta strandi207 – 2148
    Beta strandi218 – 2258
    Beta strandi237 – 2448
    Beta strandi250 – 2556
    Beta strandi259 – 27012
    Beta strandi273 – 28210
    Beta strandi285 – 2895
    Helixi290 – 2923
    Helixi300 – 3023
    Beta strandi326 – 3294
    Helixi335 – 3384
    Beta strandi339 – 3435
    Beta strandi346 – 3494
    Helixi358 – 3603
    Helixi363 – 3653
    Beta strandi375 – 3784
    Turni379 – 3824
    Beta strandi383 – 3864

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FCHX-ray1.30A/B171-387[»]
    4FEMX-ray2.50A35-387[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni174 – 283110Carbohydrate binding module (CBM) 1Add
    BLAST
    Regioni284 – 387104Carbohydrate binding module (CBM) 2Add
    BLAST
    Regioni350 – 3556Glucose binding

    Domaini

    The carbohydrate binding modules (CBM) mediate starch-binding.1 Publication

    Sequence similaritiesi

    Belongs to the SusE family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiTEHTINI.
    OrthoDBiEOG6H4K93.

    Family and domain databases

    InterProiIPR025970. SusE.
    [Graphical view]
    PfamiPF14292. SusE. 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.

    G8JZT0-1 [UniParc]FASTAAdd to Basket

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    MKKISNILLA VTFALPLFTA CETDNDSNPI LNEPDTFTLN TPAYAANNVY    50
    DLKNAQTVEL TCSQPDYGFP AATTYTVQAS FEQDFIEATD ESKANYTVLE 100
    STSPTAKINV DASELNNALL DLWTAVNGEQ AELPTEPVAV YIRLKANITS 150
    SGKGVCFSNV IELPNVLISK STSSLTPPKT MFIVGSMLDT DWKVWKPMAG 200
    VYGMDGQFYS MIYFDANSEF KFGTKENEYI GINDNRVTVT DKAGAGVSGS 250
    DNFVVENAGW YLFYVKAAVK GDDYQFTITF YPAEVYLFGN TTGGSWAFND 300
    EWKFTVPATK DGNFVSPAMT ASGEVRMCFK TDLDWWRTEF TLHDGEIFYR 350
    DFNLIDSWTE KGDGYSIQGS AGNVIHLNFT AGTGEKK 387
    Length:387
    Mass (Da):42,755
    Last modified:January 25, 2012 - v1
    Checksum:iD6D0620E02BE6980
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77615 Genomic DNA. Translation: AAB42171.1.
    AE015928 Genomic DNA. Translation: AAO78805.1.
    RefSeqiNP_812611.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO78805; AAO78805; BT_3700.
    GeneIDi1076278.
    KEGGibth:BT_3700.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77615 Genomic DNA. Translation: AAB42171.1 .
    AE015928 Genomic DNA. Translation: AAO78805.1 .
    RefSeqi NP_812611.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FCH X-ray 1.30 A/B 171-387 [» ]
    4FEM X-ray 2.50 A 35-387 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO78805 ; AAO78805 ; BT_3700 .
    GeneIDi 1076278.
    KEGGi bth:BT_3700.

    Phylogenomic databases

    OMAi TEHTINI.
    OrthoDBi EOG6H4K93.

    Enzyme and pathway databases

    UniPathwayi UPA00153 .
    BioCyci BTHE226186:GJXV-3766-MONOMER.

    Family and domain databases

    InterProi IPR025970. SusE.
    [Graphical view ]
    Pfami PF14292. SusE. 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.
      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. "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 SUSF.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    4. "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.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    5. "Multidomain carbohydrate-binding proteins involved in bacteroides thetaiotaomicron starch metabolism."
      Cameron E.A., Maynard M.A., Smith C.J., Smith T.J., Koropatkin N.M., Martens E.C.
      J. Biol. Chem. 287:34614-34625(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-387 IN COMPLEX WITH ALPHA-D-GLUCOSE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, STARCH-BINDING, PALMITOYLATION AT CYS-21, MUTAGENESIS OF CYS-21; TRP-192; LYS-221; TYR-229; ASN-252; ARG-326; TRP-336 AND ARG-350.
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

    Entry informationi

    Entry nameiSUSE_BACTN
    AccessioniPrimary (citable) accession number: G8JZT0
    Secondary accession number(s): Q45769, Q7C3Z3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: January 25, 2012
    Last modified: October 1, 2014
    This is version 18 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