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Protein

Serralysin

Gene
N/A
Organism
Serratia marcescens (strain ATCC 21074 / E-15)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 7 Ca2+ ions per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi192Zinc; catalytic1
Active sitei1931
Metal bindingi196Zinc; catalytic1
Metal bindingi202Zinc; catalytic1
Metal bindingi232Zinc; catalytic1
Metal bindingi269Calcium 1; via carbonyl oxygen1
Metal bindingi271Calcium 1; via carbonyl oxygen1
Metal bindingi273Calcium 11
Metal bindingi301Calcium 11
Metal bindingi303Calcium 1; via carbonyl oxygen1
Metal bindingi304Calcium 2; via carbonyl oxygen1
Metal bindingi306Calcium 11
Metal bindingi306Calcium 21
Metal bindingi343Calcium 2; via carbonyl oxygen1
Metal bindingi345Calcium 21
Metal bindingi350Calcium 3; via carbonyl oxygen1
Metal bindingi352Calcium 3; via carbonyl oxygen1
Metal bindingi354Calcium 31
Metal bindingi359Calcium 4; via carbonyl oxygen1
Metal bindingi361Calcium 4; via carbonyl oxygen1
Metal bindingi363Calcium 41
Metal bindingi367Calcium 3; via carbonyl oxygen1
Metal bindingi368Calcium 5; via carbonyl oxygen1
Metal bindingi369Calcium 3; via carbonyl oxygen1
Metal bindingi372Calcium 31
Metal bindingi372Calcium 51
Metal bindingi376Calcium 4; via carbonyl oxygen1
Metal bindingi377Calcium 6; via carbonyl oxygen1
Metal bindingi378Calcium 4; via carbonyl oxygen1
Metal bindingi379Calcium 6; via carbonyl oxygen1
Metal bindingi381Calcium 41
Metal bindingi381Calcium 61
Metal bindingi385Calcium 5; via carbonyl oxygen1
Metal bindingi386Calcium 7; via carbonyl oxygen1
Metal bindingi387Calcium 5; via carbonyl oxygen1
Metal bindingi388Calcium 7; via carbonyl oxygen1
Metal bindingi390Calcium 51
Metal bindingi390Calcium 71
Metal bindingi399Calcium 61
Metal bindingi406Calcium 61
Metal bindingi416Calcium 71

GO - Molecular functioni

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000286951 – 161 PublicationAdd BLAST16
ChainiPRO_000002869617 – 487SerralysinAdd BLAST471

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 29Combined sources9
Turni30 – 32Combined sources3
Beta strandi39 – 44Combined sources6
Helixi48 – 55Combined sources8
Turni56 – 58Combined sources3
Beta strandi72 – 77Combined sources6
Helixi99 – 115Combined sources17
Beta strandi116 – 122Combined sources7
Beta strandi125 – 127Combined sources3
Beta strandi130 – 136Combined sources7
Beta strandi138 – 140Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi167 – 171Combined sources5
Helixi175 – 178Combined sources4
Turni180 – 182Combined sources3
Helixi184 – 197Combined sources14
Beta strandi208 – 211Combined sources4
Helixi215 – 217Combined sources3
Turni225 – 227Combined sources3
Helixi235 – 238Combined sources4
Helixi252 – 262Combined sources11
Turni266 – 269Combined sources4
Beta strandi274 – 276Combined sources3
Helixi284 – 286Combined sources3
Beta strandi297 – 299Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi318 – 320Combined sources3
Beta strandi326 – 328Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi346 – 348Combined sources3
Beta strandi355 – 357Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi373 – 375Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi391 – 393Combined sources3
Helixi397 – 400Combined sources4
Beta strandi406 – 410Combined sources5
Turni413 – 415Combined sources3
Beta strandi416 – 419Combined sources4
Helixi421 – 427Combined sources7
Beta strandi432 – 435Combined sources4
Beta strandi445 – 451Combined sources7
Turni452 – 455Combined sources4
Beta strandi456 – 461Combined sources6
Beta strandi470 – 477Combined sources8
Turni481 – 483Combined sources3
Beta strandi484 – 486Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SRPX-ray2.00A17-487[»]
ProteinModelPortaliP07268.
SMRiP07268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07268.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati348 – 365Hemolysin-type calcium-binding 1Add BLAST18
Repeati366 – 383Hemolysin-type calcium-binding 2Add BLAST18

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.
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]
PfamiPF00413. 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 differs from that shown. Reason: Frameshift at positions 350 and 355.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04127 Genomic DNA. Translation: CAA27738.1. Frameshift.
PIRiA23596. HYSE15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04127 Genomic DNA. Translation: CAA27738.1. Frameshift.
PIRiA23596. HYSE15.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SRPX-ray2.00A17-487[»]
ProteinModelPortaliP07268.
SMRiP07268.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.051.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07268.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
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]
PfamiPF00413. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.