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Protein

Outer membrane protein SusE

Gene

susE

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

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: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei326 – 3261Glucose
Binding sitei335 – 3351Glucose

GO - Molecular functioni

  • starch binding Source: MENGO

GO - Biological processi

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
Proteomesi
  • UP000001414 Componenti: Chromosome

Subcellular locationi

  • Cell outer membrane 1 Publication; Lipid-anchor PROSITE-ProRule annotation1 Publication

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

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

Proteomic databases

PaxDbiG8JZT0.

Expressioni

Inductioni

By maltose.1 Publication

Interactioni

Subunit structurei

Monomer (Probable). Interacts with SusF.Curated2 Publications

Protein-protein interaction databases

STRINGi226186.BT_3700.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiENOG4106MPV. Bacteria.
ENOG410YCXJ. LUCA.
HOGENOMiHOG000133176.
OMAiVELTCSQ.
OrthoDBiPOG091H1JJS.

Family and domain databases

InterProiIPR025970. SusE.
IPR032187. SusF/SusE.
[Graphical view]
PfamiPF16411. DUF5019. 1 hit.
PF14292. 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

        10         20         30         40         50
MKKISNILLA VTFALPLFTA CETDNDSNPI LNEPDTFTLN TPAYAANNVY
60 70 80 90 100
DLKNAQTVEL TCSQPDYGFP AATTYTVQAS FEQDFIEATD ESKANYTVLE
110 120 130 140 150
STSPTAKINV DASELNNALL DLWTAVNGEQ AELPTEPVAV YIRLKANITS
160 170 180 190 200
SGKGVCFSNV IELPNVLISK STSSLTPPKT MFIVGSMLDT DWKVWKPMAG
210 220 230 240 250
VYGMDGQFYS MIYFDANSEF KFGTKENEYI GINDNRVTVT DKAGAGVSGS
260 270 280 290 300
DNFVVENAGW YLFYVKAAVK GDDYQFTITF YPAEVYLFGN TTGGSWAFND
310 320 330 340 350
EWKFTVPATK DGNFVSPAMT ASGEVRMCFK TDLDWWRTEF TLHDGEIFYR
360 370 380
DFNLIDSWTE KGDGYSIQGS AGNVIHLNFT AGTGEKK
Length:387
Mass (Da):42,755
Last modified:January 25, 2012 - v1
Checksum:iD6D0620E02BE6980
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77615 Genomic DNA. Translation: AAB42171.1.
AE015928 Genomic DNA. Translation: AAO78805.1.
RefSeqiNP_812611.1. NC_004663.1.
WP_008767006.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO78805; AAO78805; BT_3700.
GeneIDi1076278.
KEGGibth:BT_3700.
PATRICi21062401. VBIBacThe70966_3760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77615 Genomic DNA. Translation: AAB42171.1.
AE015928 Genomic DNA. Translation: AAO78805.1.
RefSeqiNP_812611.1. NC_004663.1.
WP_008767006.1. NC_004663.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi226186.BT_3700.

Proteomic databases

PaxDbiG8JZT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO78805; AAO78805; BT_3700.
GeneIDi1076278.
KEGGibth:BT_3700.
PATRICi21062401. VBIBacThe70966_3760.

Phylogenomic databases

eggNOGiENOG4106MPV. Bacteria.
ENOG410YCXJ. LUCA.
HOGENOMiHOG000133176.
OMAiVELTCSQ.
OrthoDBiPOG091H1JJS.

Enzyme and pathway databases

UniPathwayiUPA00153.
BioCyciBTHE226186:GJXV-3766-MONOMER.

Family and domain databases

InterProiIPR025970. SusE.
IPR032187. SusF/SusE.
[Graphical view]
PfamiPF16411. DUF5019. 1 hit.
PF14292. SusE. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 24 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.