Streptavidin precursor - Streptomyces avidinii

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P22629 (SAV_STRAV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Streptavidin
Organism	Streptomyces avidinii
Taxonomic identifier	1895 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
Subunit structure	Homotetramer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the avidin/streptavidin family. Contains 1 avidin-like domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Biotin
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Ref.1

Chain

25 – 183

159

Streptavidin

PRO_0000002729

Regions

Domain

37 – 159

123

Avidin-like

Motif

83 – 85

Cell attachment site; atypical

Sites

Binding site

Biotin

Binding site

Biotin

Binding site

116

Biotin

Binding site

132

Biotin

Binding site

144

Biotin

Secondary structure

183

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22629 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 4652D8AE018468F5
Show »

FASTA

183

18,834

        10         20         30         40         50         60 
MRKIVVAAIA VSLTTVSITA SASADPSKDS KAQVSAAEAG ITGTWYNQLG STFIVTAGAD 

        70         80         90        100        110        120 
GALTGTYESA VGNAESRYVL TGRYDSAPAT DGSGTALGWT VAWKNNYRNA HSATTWSGQY 

       130        140        150        160        170        180 
VGGAEARINT QWLLTSGTTE ANAWKSTLVG HDTFTKVKPS AASIDAAKKA GVNNGNPLDA 


VQQ

« Hide

References

[1]	"Molecular cloning and nucleotide sequence of the streptavidin gene." Argarana C.E., Kuntz I.D., Birken S., Axel R., Cantor C.R. Nucleic Acids Res. 14:1871-1882(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64.
[2]	"Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site." Gitlin G., Bayer E.A., Wilchek M. Biochem. J. 256:279-282(1988) [PubMed] [Europe PMC] [Abstract] Cited for: IMPORTANCE OF TRP IN BIOTIN-BINDING.
[3]	"Studies on the biotin-binding sites of avidin and streptavidin. Tyrosine residues are involved in the binding site." Gitlin G., Bayer E.A., Wilchek M. Biochem. J. 269:527-530(1990) [PubMed] [Europe PMC] [Abstract] Cited for: IMPORTANCE OF TYR IN BIOTIN-BINDING.
[4]	"Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin." Alon R., Bayer E.A., Wilchek M. Biochem. Biophys. Res. Commun. 170:1236-1241(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CELL-BINDING.
[5]	"Structural origins of high-affinity biotin binding to streptavidin." Weber P.C., Ohlendorf D.H., Wendoloski J.J., Salemme F.R. Science 243:85-88(1989) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 37-157.
[6]	"Structural studies of the streptavidin binding loop." Freitag S., le Trong I., Klumb L., Stayton P.S., Stenkamp R.E. Protein Sci. 6:1157-1166(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-157.
[7]	"In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0." Katz B.A., Cass R.T. J. Biol. Chem. 272:13220-13228(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 37-157.
[8]	"Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH." Katz B.A. J. Mol. Biol. 274:776-800(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 37-157.
[9]	"Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex." Freitag S., le Trong I., Chilkoti A., Klumb L.A., Stayton P.S., Stenkamp R.E. J. Mol. Biol. 279:211-221(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-157 OF MUTANTS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03591 Genomic DNA. Translation: CAA27265.1.

PIR

A23513.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DF8	X-ray	1.51	A/B	37-163	[»]
1HQQ	X-ray	1.70	A/B/C/D	36-163	[»]
1HXL	X-ray	1.80	A/B	36-163	[»]
1HXZ	X-ray	1.80	A/B	36-163	[»]
1HY2	X-ray	2.00	A/B/C/D	36-163	[»]
1I9H	X-ray	2.40	A/B	25-163	[»]
1KFF	X-ray	1.90	A/B/C/D	38-163	[»]
1KL3	X-ray	1.70	A/B/C/D	38-163	[»]
1KL4	X-ray	1.70	A/B/C/D	38-163	[»]
1KL5	X-ray	1.80	A/B/C/D	38-163	[»]
1LCV	X-ray	2.30	A/B	39-159	[»]
1LCW	X-ray	2.20	A/B	39-159	[»]
1LCZ	X-ray	1.95	A/B	25-159	[»]
1LUQ	X-ray	0.96	A/B	37-163	[»]
1MEP	X-ray	1.65	A/B/C/D	37-163	[»]
1MK5	X-ray	1.40	A/B	37-163	[»]
1MM9	X-ray	1.66	A	37-163	[»]
1MOY	X-ray	1.55	A	37-163	[»]
1N43	X-ray	1.89	A/B/C/D	37-163	[»]
1N4J	X-ray	2.18	A	37-163	[»]
1N7Y	X-ray	1.96	A/B/C/D	37-163	[»]
1N9M	X-ray	1.60	A/B/C/D	37-163	[»]
1N9Y	X-ray	1.53	A/B/C/D	37-163	[»]
1NBX	X-ray	1.70	A/B/C/D	37-163	[»]
1NC9	X-ray	1.80	A/B/C/D	37-163	[»]
1NDJ	X-ray	1.81	A/B/C/D	37-163	[»]
1NQM	X-ray	1.70	A/B/C/D	24-159	[»]
1PTS	X-ray	2.00	A/B	37-157	[»]
1RST	X-ray	1.70	B	38-163	[»]
1RSU	X-ray	1.70	B	38-163	[»]
1RXH	X-ray	2.90	A/B	37-163	[»]
1RXJ	X-ray	1.14	A/B/C/D	39-159	[»]
1RXK	X-ray	1.70	A/B	38-159	[»]
1SLD	X-ray	2.50	B	25-159	[»]
1SLE	X-ray	2.00	B/D	25-159	[»]
1SLF	X-ray	1.76	B/D	25-159	[»]
1SLG	X-ray	1.76	B/D	25-159	[»]
1SRE	X-ray	1.78	A/B	37-157	[»]
1SRF	X-ray	2.00	A/B	37-157	[»]
1SRG	X-ray	1.80	A/B	37-157	[»]
1SRH	X-ray	2.20	A/B	37-157	[»]
1SRI	X-ray	1.65	A/B	37-157	[»]
1SRJ	X-ray	1.80	A/B	37-157	[»]
1STP	X-ray	2.60	A	25-183	[»]
1STR	X-ray	1.80	B/D	37-159	[»]
1STS	X-ray	1.95	B/D	37-159	[»]
1SWA	X-ray	1.90	A/B/C/D	37-163	[»]
1SWB	X-ray	1.85	A/B/C/D	37-163	[»]
1SWC	X-ray	1.80	A/B/C/D	37-163	[»]
1SWD	X-ray	1.90	A/B/C/D	37-163	[»]
1SWE	X-ray	2.06	A/B/C/D	37-163	[»]
1SWF	X-ray	2.00	A/B/C/D	37-163	[»]
1SWG	X-ray	1.80	A/B/C/D	37-163	[»]
1SWH	X-ray	1.70	A/B/C/D	37-163	[»]
1SWJ	X-ray	2.00	A/B/C/D	37-163	[»]
1SWK	X-ray	2.00	A/B/C/D	37-163	[»]
1SWL	X-ray	1.80	A/B/C/D	37-163	[»]
1SWN	X-ray	2.20	A/B/C/D	37-163	[»]
1SWO	X-ray	1.95	A/B/C/D	37-163	[»]
1SWP	X-ray	2.00	A/B/C/D	37-163	[»]
1SWQ	X-ray	1.90	A/B/C/D	37-163	[»]
1SWR	X-ray	1.90	A/B/C/D	37-163	[»]
1SWS	X-ray	2.00	A/B/C/D	37-163	[»]
1SWT	X-ray	2.00	A/B	37-163	[»]
1SWU	X-ray	1.14	A/B/C/D	37-163	[»]
1VWA	X-ray	1.85	B/D	37-159	[»]
1VWB	X-ray	1.82	B	37-159	[»]
1VWC	X-ray	1.86	B	37-159	[»]
1VWD	X-ray	1.87	B	37-159	[»]
1VWE	X-ray	1.50	B	37-159	[»]
1VWF	X-ray	1.92	B	37-159	[»]
1VWG	X-ray	1.46	B	37-159	[»]
1VWH	X-ray	1.48	B	37-159	[»]
1VWI	X-ray	1.50	B/D	37-159	[»]
1VWJ	X-ray	1.45	B/D	37-159	[»]
1VWK	X-ray	1.45	B/D	37-159	[»]
1VWL	X-ray	1.45	B/D	37-159	[»]
1VWM	X-ray	1.60	B	37-159	[»]
1VWN	X-ray	1.85	B	37-159	[»]
1VWO	X-ray	1.65	B	37-159	[»]
1VWP	X-ray	1.75	B	37-159	[»]
1VWQ	X-ray	1.70	B	37-159	[»]
1VWR	X-ray	1.50	B	37-159	[»]
2BC3	X-ray	1.54	A/B	38-183	[»]
2F01	X-ray	0.85	A/B	37-163	[»]
2G5L	X-ray	1.15	A/B	37-163	[»]
2GH7	X-ray	1.00	A/B	37-163	[»]
2IZA	X-ray	1.46	A	37-157	[»]
2IZB	X-ray	1.20	A	37-158	[»]
2IZC	X-ray	1.40	B/D	37-159	[»]
2IZD	X-ray	1.60	B/D	37-159	[»]
2IZE	X-ray	1.57	B/D	37-159	[»]
2IZF	X-ray	1.58	B/D	37-159	[»]
2IZG	X-ray	1.36	B/D	37-159	[»]
2IZH	X-ray	1.36	B/D	37-159	[»]
2IZI	X-ray	1.50	A	37-159	[»]
2IZJ	X-ray	1.30	A	37-159	[»]
2IZK	X-ray	1.30	A	37-159	[»]
2IZL	X-ray	1.48	B/D	37-159	[»]
2QCB	X-ray	1.65	A	38-183	[»]
2RTA	X-ray	1.39	A	25-159	[»]
2RTB	X-ray	1.50	B/D	25-159	[»]
2RTC	X-ray	1.50	B/D	25-159	[»]
2RTD	X-ray	1.65	B/D	25-159	[»]
2RTE	X-ray	1.50	B/D	25-159	[»]
2RTF	X-ray	1.47	B/D	25-159	[»]
2RTG	X-ray	1.39	B/D	25-159	[»]
2RTH	X-ray	1.56	B/D	25-159	[»]
2RTI	X-ray	1.40	B/D	25-159	[»]
2RTJ	X-ray	1.40	A	25-159	[»]
2RTK	X-ray	1.82	A	25-159	[»]
2RTL	X-ray	1.41	A	25-159	[»]
2RTM	X-ray	1.30	A	25-159	[»]
2RTN	X-ray	1.80	B/D	25-159	[»]
2RTO	X-ray	1.58	B/D	25-159	[»]
2RTP	X-ray	1.50	B/D	25-159	[»]
2RTQ	X-ray	1.39	B/D	25-159	[»]
2RTR	X-ray	1.62	B/D	25-159	[»]
2WPU	X-ray	1.92	A	38-183	[»]
2Y3E	X-ray	1.45	A/B	37-163	[»]
2Y3F	X-ray	1.49	A	37-163	[»]
3MG5	X-ray	1.30	A/B/C/D	37-163	[»]
3PK2	X-ray	1.90	A	38-183	[»]
3RDM	X-ray	1.60	A	37-164	[»]
3RDO	X-ray	1.40	A	37-164	[»]
3RDQ	X-ray	1.60	A	37-164	[»]
3RDS	X-ray	1.50	A	37-164	[»]
3RDU	X-ray	1.50	A	37-164	[»]
3RDX	X-ray	2.10	A/B	37-164	[»]
3RE5	X-ray	1.95	A	37-164	[»]
3RE6	X-ray	1.82	A	37-164	[»]
3RY1	X-ray	1.03	A/B/C/D	37-163	[»]
3RY2	X-ray	0.95	A/B	37-163	[»]
3T6F	X-ray	1.22	A/B	37-163	[»]
3T6L	X-ray	1.30	A	37-163	[»]
4DNE	X-ray	1.88	A/B	1-183	[»]
4EKV	X-ray	2.00	A	25-183	[»]
4GJS	X-ray	1.85	A/B	38-183	[»]
4GJV	X-ray	2.40	A	38-183	[»]

ProteinModelPortal

P22629.

SMR

P22629. Positions 38-159.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.40.128.30. 1 hit.

InterPro

IPR005469. Avidin.
IPR017889. Avidin-like_CS.
IPR005468. Avidin/str.
[Graphical view]

Pfam

PF01382. Avidin. 1 hit.
[Graphical view]

PRINTS

PR00709. AVIDIN.

SUPFAM

SSF50876. Avidin/str. 1 hit.

PROSITE

PS00577. AVIDIN_1. 1 hit.
PS51326. AVIDIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075026.

EvolutionaryTrace

P22629.

Entry information

Entry name

SAV_STRAV

Accession

Primary (citable) accession number: P22629

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents