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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)DescriptionActionsGraphical viewLength
Binding sitei326Glucose1
Binding sitei335Glucose1

GO - Molecular functioni

  • starch binding Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi21C → A: Abolishes cell outer membrane localization. 1 Publication1
Mutagenesisi192W → 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 Publication1
Mutagenesisi221K → 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 Publication1
Mutagenesisi229Y → 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 Publication1
Mutagenesisi252N → 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 Publication1
Mutagenesisi326R → 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 Publication1
Mutagenesisi336W → 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 Publication1
Mutagenesisi350R → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20PROSITE-ProRule annotationAdd BLAST20
ChainiPRO_000042588921 – 387Outer membrane protein SusEAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi21N-palmitoyl cysteine1 Publication1
Lipidationi21S-diacylglycerol cysteineCurated1

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

1387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi182 – 185Combined sources4
Turni186 – 188Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi207 – 214Combined sources8
Beta strandi218 – 225Combined sources8
Beta strandi237 – 244Combined sources8
Beta strandi250 – 255Combined sources6
Beta strandi259 – 270Combined sources12
Beta strandi273 – 282Combined sources10
Beta strandi285 – 289Combined sources5
Helixi290 – 292Combined sources3
Helixi300 – 302Combined sources3
Beta strandi326 – 329Combined sources4
Helixi335 – 338Combined sources4
Beta strandi339 – 343Combined sources5
Beta strandi346 – 349Combined sources4
Helixi358 – 360Combined sources3
Helixi363 – 365Combined sources3
Beta strandi375 – 378Combined sources4
Turni379 – 382Combined sources4
Beta strandi383 – 386Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FCHX-ray1.30A/B171-387[»]
4FEMX-ray2.50A35-387[»]
SMRiG8JZT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 283Carbohydrate binding module (CBM) 1Add BLAST110
Regioni284 – 387Carbohydrate binding module (CBM) 2Add BLAST104
Regioni350 – 355Glucose binding6

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]
PfamiPF14292. SusE. 1 hit.
PF16411. SusF_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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FCHX-ray1.30A/B171-387[»]
4FEMX-ray2.50A35-387[»]
SMRiG8JZT0.
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.

Family and domain databases

InterProiIPR025970. SusE.
IPR032187. SusF/SusE.
[Graphical view]
PfamiPF14292. SusE. 1 hit.
PF16411. SusF_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: November 2, 2016
This is version 26 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.