Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P22266

- ESTA_STRSC

UniProt

P22266 - ESTA_STRSC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Esterase

Gene

estA

Organism
Streptomyces scabiei
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Names & Taxonomyi

Protein namesi
Recommended name:
Esterase (EC:3.1.1.-)
Gene namesi
Name:estA
OrganismiStreptomyces scabiei
Taxonomic identifieri1930 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 39391 PublicationAdd
BLAST
Chaini40 – 345306EsterasePRO_0000021208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi73 ↔ 103
Disulfide bondi156 ↔ 180
Disulfide bondi236 ↔ 294

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By zinc.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496Combined sources
Helixi53 – 564Combined sources
Turni57 – 593Combined sources
Beta strandi61 – 633Combined sources
Turni64 – 674Combined sources
Helixi69 – 735Combined sources
Helixi80 – 8910Combined sources
Turni90 – 923Combined sources
Beta strandi94 – 1007Combined sources
Helixi108 – 1114Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 1203Combined sources
Beta strandi122 – 1243Combined sources
Helixi127 – 1304Combined sources
Beta strandi137 – 1404Combined sources
Helixi144 – 1474Combined sources
Helixi149 – 1557Combined sources
Turni158 – 1614Combined sources
Beta strandi171 – 1755Combined sources
Helixi177 – 1793Combined sources
Helixi180 – 1834Combined sources
Turni184 – 1863Combined sources
Helixi188 – 21427Combined sources
Beta strandi219 – 2235Combined sources
Helixi233 – 2375Combined sources
Turni247 – 2504Combined sources
Turni253 – 2553Combined sources
Helixi256 – 27520Combined sources
Turni276 – 2783Combined sources
Beta strandi280 – 2823Combined sources
Helixi285 – 2873Combined sources
Beta strandi304 – 31411Combined sources
Beta strandi316 – 3183Combined sources
Helixi325 – 34218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ESCX-ray2.10A40-345[»]
1ESDX-ray2.30A40-345[»]
1ESEX-ray2.40A40-345[»]
ProteinModelPortaliP22266.
SMRiP22266. Positions 43-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22266.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22266-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSAMRKTTN SPVVRRLTAA AVALGSCLAL AGPAGSAGAA PADPVPTVFF
60 70 80 90 100
GDSYTANFGI APVTNQDSER GWCFQAKENY PAVATRSLAD KGITLDVQAD
110 120 130 140 150
VSCGGALIHH FWEKQELPFG AGELPPQQDA LKQDTQLTVG SLGGNTLGFN
160 170 180 190 200
RILKQCSDEL RKPSLLPGDP VDGDEPAAKC GEFFGTGDGK QWLDDQFERV
210 220 230 240 250
GAELEELLDR IGYFAPDAKR VLVGYPRLVP EDTTKCLTAA PGQTQLPFAD
260 270 280 290 300
IPQDALPVLD QIQKRLNDAM KKAAADGGAD FVDLYAGTGA NTACDGADRG
310 320 330 340
IGGLLEDSQL ELLGTKIPWY AHPNDKGRDI QAKQVADKIE EILNR
Length:345
Mass (Da):36,670
Last modified:August 1, 1991 - v1
Checksum:i237DC28EE185B00E
GO

Sequence cautioni

The sequence AAA26744.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57297 Genomic DNA. Translation: AAA26743.1.
M57297 Genomic DNA. Translation: AAA26744.1. Different initiation.
PIRiA37845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57297 Genomic DNA. Translation: AAA26743.1 .
M57297 Genomic DNA. Translation: AAA26744.1 . Different initiation.
PIRi A37845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ESC X-ray 2.10 A 40-345 [» ]
1ESD X-ray 2.30 A 40-345 [» ]
1ESE X-ray 2.40 A 40-345 [» ]
ProteinModelPortali P22266.
SMRi P22266. Positions 43-344.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P22266.

Family and domain databases

Gene3Di 3.40.50.1110. 1 hit.
InterProi IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequencing, and regulation of expression of an extracellular esterase gene from the plant pathogen Streptomyces scabies."
    Raymer G., Willard J.M.A., Schottel J.L.
    J. Bacteriol. 172:7020-7026(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-69.
    Strain: FL1.
  2. "Regulation and secretion of an extracellular esterase from Streptomyces scabies."
    Schottel J.L., Hale V., Babcock M.J.
    Gene 115:27-31(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "A novel variant of the catalytic triad in the Streptomyces scabies esterase."
    Wei Y., Schottel J.L., Derewenda U., Swenson L., Patkar S., Derewenda Z.S.
    Nat. Struct. Biol. 2:218-223(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiESTA_STRSC
AccessioniPrimary (citable) accession number: P22266
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 26, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3