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Protein

Serralysin

Gene
N/A
Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death.1 Publication

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'.1 Publication

Cofactori

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

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 bindingi370Calcium 5; 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

  • calcium ion binding Source: UniProtKB
  • metalloendopeptidase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • pathogenesis Source: UniProtKB
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease, Toxin

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
Zinc proteinase
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: InterPro
  • extracellular region Source: UniProtKB
  • extracellular space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000286931 – 16Add BLAST16
ChainiPRO_000002869417 – 487SerralysinAdd BLAST471

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiP23694.

Interactioni

Protein-protein interaction databases

MINTiMINT-1508955.

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
Helixi48 – 55Combined sources8
Turni56 – 58Combined sources3
Beta strandi72 – 77Combined sources6
Helixi99 – 115Combined sources17
Beta strandi116 – 122Combined sources7
Beta strandi130 – 136Combined sources7
Beta strandi138 – 140Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi167 – 171Combined sources5
Helixi175 – 178Combined sources4
Turni180 – 182Combined sources3
Helixi184 – 198Combined sources15
Beta strandi203 – 205Combined sources3
Helixi207 – 209Combined sources3
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 strandi407 – 410Combined sources4
Turni413 – 415Combined sources3
Beta strandi417 – 419Combined sources3
Helixi421 – 427Combined sources7
Beta strandi432 – 435Combined sources4
Beta strandi445 – 451Combined sources7
Turni452 – 455Combined sources4
Beta strandi456 – 461Combined sources6
Beta strandi463 – 465Combined sources3
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
1AF0X-ray1.80A17-487[»]
1SATX-ray1.75A17-487[»]
1SMPX-ray2.30A17-487[»]
4I35X-ray1.50A19-487[»]
5D7WX-ray1.10A20-487[»]
ProteinModelPortaliP23694.
SMRiP23694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23694.

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.

P23694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSTKKAIEI TESSLAAATT 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 GNPTYNDVTY AEDTRQFSLM SYWSETNTGG DNGGHYAAAP
260 270 280 290 300
LLDDIAAIQH LYGANPSTRT 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 SFFNKEANSS DFIHFVDHFS GTAGEALLSY
460 470 480
NASSNVTDLS VNIGGHQAPD FLVKIVGQVD VATDFIV
Length:487
Mass (Da):52,105
Last modified:November 1, 1991 - v1
Checksum:i8689FC84D83CAA2C
GO

Sequence cautioni

The sequence CAA39138 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA39139 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14S → E AA sequence (PubMed:16391997).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55521 Genomic DNA. Translation: CAA39137.1.
X55521 Genomic DNA. Translation: CAA39138.1. Different initiation.
X55521 Genomic DNA. Translation: CAA39139.1. Different initiation.
PIRiS12164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55521 Genomic DNA. Translation: CAA39137.1.
X55521 Genomic DNA. Translation: CAA39138.1. Different initiation.
X55521 Genomic DNA. Translation: CAA39139.1. Different initiation.
PIRiS12164.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AF0X-ray1.80A17-487[»]
1SATX-ray1.75A17-487[»]
1SMPX-ray2.30A17-487[»]
4I35X-ray1.50A19-487[»]
5D7WX-ray1.10A20-487[»]
ProteinModelPortaliP23694.
SMRiP23694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1508955.

Protein family/group databases

MEROPSiM10.051.

Proteomic databases

PRIDEiP23694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23694.

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_SERMA
AccessioniPrimary (citable) accession number: P23694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 109 of the entry and version 1 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.

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.