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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)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 bindingi370 – 3701Calcium 5; 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

  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

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)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1616PRO_0000028693Add
BLAST
Chaini17 – 487471SerralysinPRO_0000028694Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Protein-protein interaction databases

MINTiMINT-1508955.

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 299Combined sources
Turni30 – 323Combined sources
Helixi48 – 558Combined sources
Turni56 – 583Combined sources
Beta strandi72 – 776Combined sources
Helixi99 – 11517Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi167 – 1715Combined sources
Helixi175 – 1784Combined sources
Turni180 – 1823Combined sources
Helixi184 – 19815Combined sources
Beta strandi203 – 2053Combined sources
Helixi207 – 2093Combined sources
Helixi215 – 2173Combined sources
Turni225 – 2273Combined sources
Helixi235 – 2384Combined sources
Helixi252 – 26211Combined sources
Turni266 – 2694Combined sources
Beta strandi274 – 2763Combined sources
Helixi284 – 2863Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi391 – 3933Combined sources
Helixi397 – 4004Combined sources
Beta strandi407 – 4104Combined sources
Turni413 – 4153Combined sources
Beta strandi417 – 4193Combined sources
Helixi421 – 4277Combined sources
Beta strandi432 – 4354Combined sources
Beta strandi445 – 4517Combined sources
Turni452 – 4554Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi470 – 4778Combined sources
Turni481 – 4833Combined sources
Beta strandi484 – 4863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 20-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23694.

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141S → E AA sequence (PubMed:16391997).Curated

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
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. Positions 20-487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1508955.

Protein family/group databases

MEROPSiM10.051.

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: May 11, 2016
This is version 107 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.