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P07268

- PRZN_SERME

UniProt

P07268 - PRZN_SERME

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Protein

Serralysin

Gene
N/A
Organism
Serratia marcescens (strain ATCC 21074 / E-15)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon.

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'.

Cofactori

Binds 7 calcium ions per subunit.
Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi192 – 1921Zinc; catalytic
Active sitei193 – 1931
Metal bindingi196 – 1961Zinc; catalytic
Metal bindingi202 – 2021Zinc; catalytic
Metal bindingi232 – 2321Zinc; catalytic
Metal bindingi269 – 2691Calcium 1; via carbonyl oxygen
Metal bindingi271 – 2711Calcium 1; via carbonyl oxygen
Metal bindingi273 – 2731Calcium 1
Metal bindingi301 – 3011Calcium 1
Metal bindingi303 – 3031Calcium 1; via carbonyl oxygen
Metal bindingi304 – 3041Calcium 2; via carbonyl oxygen
Metal bindingi306 – 3061Calcium 1
Metal bindingi306 – 3061Calcium 2
Metal bindingi343 – 3431Calcium 2; via carbonyl oxygen
Metal bindingi345 – 3451Calcium 2
Metal bindingi350 – 3501Calcium 3; via carbonyl oxygen
Metal bindingi352 – 3521Calcium 3; via carbonyl oxygen
Metal bindingi354 – 3541Calcium 3
Metal bindingi359 – 3591Calcium 4; via carbonyl oxygen
Metal bindingi361 – 3611Calcium 4; via carbonyl oxygen
Metal bindingi363 – 3631Calcium 4
Metal bindingi367 – 3671Calcium 3; via carbonyl oxygen
Metal bindingi368 – 3681Calcium 5; via carbonyl oxygen
Metal bindingi369 – 3691Calcium 3; via carbonyl oxygen
Metal bindingi372 – 3721Calcium 3
Metal bindingi372 – 3721Calcium 5
Metal bindingi376 – 3761Calcium 4; via carbonyl oxygen
Metal bindingi377 – 3771Calcium 6; via carbonyl oxygen
Metal bindingi378 – 3781Calcium 4; via carbonyl oxygen
Metal bindingi379 – 3791Calcium 6; via carbonyl oxygen
Metal bindingi381 – 3811Calcium 4
Metal bindingi381 – 3811Calcium 6
Metal bindingi385 – 3851Calcium 5; via carbonyl oxygen
Metal bindingi386 – 3861Calcium 7; via carbonyl oxygen
Metal bindingi387 – 3871Calcium 5; via carbonyl oxygen
Metal bindingi388 – 3881Calcium 7; via carbonyl oxygen
Metal bindingi390 – 3901Calcium 5
Metal bindingi390 – 3901Calcium 7
Metal bindingi399 – 3991Calcium 6
Metal bindingi406 – 4061Calcium 6
Metal bindingi416 – 4161Calcium 7

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.051.

Names & Taxonomyi

Protein namesi
Recommended name:
Serralysin (EC:3.4.24.40)
Alternative name(s):
Extracellular metalloproteinase
Serratiopeptidase
Short name:
Serrapeptase
Short name:
Serrapeptidase
Zinc proteinase
OrganismiSerratia marcescens (strain ATCC 21074 / E-15)
Taxonomic identifieri617 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. extracellular space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 16161 PublicationPRO_0000028695Add
BLAST
Chaini17 – 487471SerralysinPRO_0000028696Add
BLAST

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 299
Turni30 – 323
Beta strandi39 – 446
Helixi48 – 558
Turni56 – 583
Beta strandi72 – 776
Helixi99 – 11517
Beta strandi116 – 1227
Beta strandi125 – 1273
Beta strandi130 – 1367
Beta strandi138 – 1403
Beta strandi150 – 1523
Beta strandi167 – 1715
Helixi175 – 1784
Turni180 – 1823
Helixi184 – 19714
Beta strandi208 – 2114
Helixi215 – 2173
Turni225 – 2273
Helixi235 – 2384
Helixi252 – 26211
Turni266 – 2694
Beta strandi274 – 2763
Helixi284 – 2863
Beta strandi297 – 2993
Beta strandi307 – 3093
Beta strandi318 – 3203
Beta strandi326 – 3283
Beta strandi336 – 3383
Beta strandi346 – 3483
Beta strandi355 – 3573
Beta strandi364 – 3663
Beta strandi373 – 3753
Beta strandi382 – 3843
Beta strandi391 – 3933
Helixi397 – 4004
Beta strandi406 – 4105
Turni413 – 4153
Beta strandi416 – 4194
Helixi421 – 4277
Beta strandi432 – 4354
Beta strandi445 – 4517
Turni452 – 4554
Beta strandi456 – 4616
Beta strandi470 – 4778
Turni481 – 4833
Beta strandi484 – 4863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRPX-ray2.00A17-487[»]
ProteinModelPortaliP07268.
SMRiP07268. Positions 20-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07268.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati348 – 36518Hemolysin-type calcium-binding 1Add
BLAST
Repeati366 – 38318Hemolysin-type calcium-binding 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M10B family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF08548. Peptidase_M10_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001205. Peptidase_M10B. 1 hit.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 1 hit.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07268-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSTKKAIEI TESNFAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ
60 70 80 90 100
AGLFITRENQ TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE
110 120 130 140 150
QQQQAKLSLQ SWADVANITF TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA
160 170 180 190 200
YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP ATEDYGRQTF THEIGHALGL
210 220 230 240 250
SHPGDYNAGE GNPTYRDVTY AEDTRQFSLM SYWSETNTGG DNGGHYAAAP
260 270 280 290 300
LLDDIAAIQH LYGANLSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW
310 320 330 340 350
DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG
360 370 380 390 400
SGNDVIVGNA ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS
410 420 430 440 450
APGASDWIRD FQKGIDKIDL SFFNKEAQSS DFIHFVDHFS GAAGEALLSY
460 470 480
NASNNVTDLS VNIGGHQAPD FLVKIVGQVD VATDFIV
Length:487
Mass (Da):52,235
Last modified:June 20, 2003 - v2
Checksum:i270A315CADD568C3
GO

Sequence cautioni

The sequence CAA27738.1 differs from that shown. Reason: Frameshift at positions 350 and 355.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04127 Genomic DNA. Translation: CAA27738.1. Frameshift.
PIRiA23596. HYSE15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04127 Genomic DNA. Translation: CAA27738.1 . Frameshift.
PIRi A23596. HYSE15.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SRP X-ray 2.00 A 17-487 [» ]
ProteinModelPortali P07268.
SMRi P07268. Positions 20-487.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.051.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07268.

Family and domain databases

Gene3Di 2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016294. Pept_M10B.
IPR013858. Peptidase_M10B_C.
IPR006026. Peptidase_Metallo.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view ]
Pfami PF00353. HemolysinCabind. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF08548. Peptidase_M10_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001205. Peptidase_M10B. 1 hit.
SMARTi SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF51120. SSF51120. 1 hit.
PROSITEi PS00330. HEMOLYSIN_CALCIUM. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Serratia protease. Amino acid sequences of both termini, the 53 residues in the middle region containing the sole methionine residue, and a probable zinc-binding region."
    Lee I.S., Wakabayashi S., Miyata K., Tomoda K., Yoneda M., Kangawa K., Minamino N., Matsuo H., Matsubara H.
    J. Biochem. 96:1409-1418(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-34 AND 179-269.
  3. "Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0-A resolution."
    Hamada K., Hata Y., Katsuya Y., Hiramatsu H., Fujiwara T., Katsube Y.
    J. Biochem. 119:844-851(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-487.

Entry informationi

Entry nameiPRZN_SERME
AccessioniPrimary (citable) accession number: P07268
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 20, 2003
Last modified: October 1, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The Gly-rich repeats may be important in the extracellular secretion of this metalloprotease.
In Japan this enzyme, isolated from a Serratia strain presents in the gut of silkworms, is used as a food supplement because it is reported to induces fibrinolytic, anti-inflammatory and anti-edemic (prevents swelling and fluid retention) activity in a number of tissues.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3