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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: -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

Keywordsi

Biological processCarbohydrate metabolism

Enzyme and pathway databases

BioCyciBTHE:G13PU-8668-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

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 cysteine1 Publication1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiG8JZT0
PRIDEiG8JZT0

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
KOiK21571
OMAiTCSQPDY
OrthoDBiPOG091H1JJS

Family and domain databases

InterProiView protein in InterPro
IPR025970 SusE
IPR032187 SusF/SusE
PfamiView protein in Pfam
PF14292 SusE, 1 hit
PF16411 SusF_SusE, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 1 hit

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
31618992
KEGGibth:BT_3700
PATRICifig|226186.12.peg.3760

Similar proteinsi

Entry informationi

Entry nameiSUSE_BACTN
AccessioniPrimary (citable) accession number: G8JZT0
Secondary accession number(s): Q45769, Q7C3Z3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: January 25, 2012
Last modified: May 23, 2018
This is version 33 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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