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P07268

- PRZN_SERME

UniProt

P07268 - PRZN_SERME

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
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (20 Jun 2003)
      Previous versions | rss
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    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

    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

    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

    MQSTKKAIEI TESNFAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ    50
    AGLFITRENQ TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE 100
    QQQQAKLSLQ SWADVANITF TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA 150
    YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP ATEDYGRQTF THEIGHALGL 200
    SHPGDYNAGE GNPTYRDVTY AEDTRQFSLM SYWSETNTGG DNGGHYAAAP 250
    LLDDIAAIQH LYGANLSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW 300
    DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG 350
    SGNDVIVGNA ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS 400
    APGASDWIRD FQKGIDKIDL SFFNKEAQSS DFIHFVDHFS GAAGEALLSY 450
    NASNNVTDLS VNIGGHQAPD FLVKIVGQVD VATDFIV 487
    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