SusD - Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)

Preferred order of sections

Names and origin

Protein names

Gene names

Name:	susD EMBL AAO78806.1
Ordered Locus Names:	BT_3701 EMBL AAO78806.1

Organism

Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP] EMBL AAO78806.1

Taxonomic identifier

226186 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides ›

Protein attributes

Sequence length	551 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC Metal-binding PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC
Technical term	3D-structure PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

73 – 75

3

Glucose binding PDB 3CK9

Region

98 – 101

4

Glucose binding PDB 3CK9

Sites

Metal binding

273

1

Calcium PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB

Metal binding

288

1

Calcium; via carbonyl oxygen PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC

Metal binding

430

1

Calcium; via carbonyl oxygen PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC

Metal binding

432

1

Calcium PDB 3CK9 PDB 3CK7 PDB 3CK8 PDB 3CKB PDB 3CKC

Binding site

81

1

Glucose PDB 3CK9

Binding site

296

1

Glucose PDB 3CK9

Binding site

320

1

Glucose PDB 3CK9

Amino acid modifications

Modified residue

322

1

Cysteine sulfenic acid (-SOH) PDB 3CKC

Sequences

Sequence

Length

Mass (Da)

Tools

Q8A1G2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EBBB322E687A5E7F
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FASTA

551

62,309

        10         20         30         40         50         60 
MKTKYIKQLF SAALIAVLSS GVTSCINDLD ISPIDPQTGG SFDQQGVFVK GYAMLGVTGQ 

        70         80         90        100        110        120 
KGIDGSPDLD GQDEGESGFY RTTFNCNELP TDECLWAWQE NQDIPQLTSI SWSPSSQRTE 

       130        140        150        160        170        180 
WVYVRLGYDI TQYNFFLDQT EGMTDAETLR QRAEIRFLRA LHYWYFLDLF GKAPFKEHFS 

       190        200        210        220        230        240 
NDLPVEKKGT ELYTYIQNEL NEIEADMYEP RQAPFGRADK AANWLLRARL YLNAGVYTGQ 

       250        260        270        280        290        300 
TDYAKAEEYA SKVIGSAYKL CTNYSELFMA DNDENENAMQ EIILPIRQDG VKTRNYGGST 

       310        320        330        340        350        360 
YLVCGTRVAG MPRMGTTNGW SCIFARAAMV QKFFSNLEDV PMLPADVEIP TKGLDTDEQI 

       370        380        390        400        410        420 
DAFDAEHGIR TEDMIKAAGD DRALLYSGVG GGRRKIQTDA ISGFTDGLSI VKWQNYRSDG 

       430        440        450        460        470        480 
KPVSHATYPD TDIPLFRLAE AYLTRAEAIF RQGGDATGDI NELRKRANCT RKVQTVTEQE 

       490        500        510        520        530        540 
LIDEWAREFY LEGRRRSDLV RFGMFTTNKY LWDWKGGAMN GTSVASYYNK YPIPVSDINN 

       550 
NRNMSQNEGY K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices." Koropatkin N.M., Martens E.C., Gordon J.I., Smith T.J. Structure 16:1105-1115(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 26-551 IN COMPLEX WITH CALCIUM AND GLUCOSE, CYSTEINE SULFENIC ACID (-SOH) AT CYS-322.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE015928 Genomic DNA. Translation: AAO78806.1.

RefSeq

NP_812612.1. NC_004663.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CK7	X-ray	2.10	A/B/C/D	26-551	[»]
3CK8	X-ray	2.10	A/B	26-551	[»]
3CK9	X-ray	2.20	A/B	26-551	[»]
3CKB	X-ray	2.30	A/B	26-551	[»]
3CKC	X-ray	1.50	A/B	26-551	[»]

ProteinModelPortal

Q8A1G2.

SMR

Q8A1G2. Positions 37-551.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46026N.

STRING

226186.BT_3701.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAO78806; AAO78806; BT_3701.

GeneID

1072099.

KEGG

bth:BT_3701.

PATRIC

21062403. VBIBacThe70966_3761.

Phylogenomic databases

HOGENOM

HOG000022810.

OMA

RTNEYGR.

ProtClustDB

CLSK823607.

Enzyme and pathway databases

BioCyc

BTHE226186:GJXV-3767-MONOMER.

Family and domain databases

Gene3D

1.25.40.10. 2 hits.

InterPro

IPR012944. SusD_RagB_dom.
IPR011990. TPR-like_helical.
[Graphical view]

Pfam

PF07980. SusD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8A1G2.

Entry information

Entry name

Q8A1G2_BACTN

Accession

Primary (citable) accession number: Q8A1G2

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)