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G8JZT0

- SUSE_BACTN

UniProt

G8JZT0 - SUSE_BACTN

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Protein

Outer membrane protein SusE

Gene
susE, BT_3700
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

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
Complete GO annotation...

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; Lipid-anchor 1 Publication

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

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 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 387367Outer membrane protein SusEPRO_0000425889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteine Inferred
Lipidationi21 – 211S-diacylglycerol cysteine Inferred

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Inductioni

By maltose.1 Publication

Interactioni

Subunit structurei

Monomer Inferred. Interacts with SusF.2 Publications

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[»]

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.

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

« Hide

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

« 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.
    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: May 14, 2014
This is version 17 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

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