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P00778

- PRLA_LYSEN

UniProt

P00778 - PRLA_LYSEN

Protein

Alpha-lytic protease

Gene

alpha-LP

Organism
Lysobacter enzymogenes
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei235 – 2351Charge relay systemBy similarity
    Active sitei262 – 2621Charge relay systemBy similarity
    Active sitei342 – 3421Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.268.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-lytic protease (EC:3.4.21.12)
    Alternative name(s):
    Alpha-lytic endopeptidase
    Gene namesi
    Name:alpha-LP
    OrganismiLysobacter enzymogenes
    Taxonomic identifieri69 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 199175PRO_0000026907Add
    BLAST
    Chaini200 – 397198Alpha-lytic proteasePRO_0000026908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi216 ↔ 236
    Disulfide bondi300 ↔ 310
    Disulfide bondi336 ↔ 369

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 4910
    Helixi53 – 553
    Helixi56 – 7722
    Helixi78 – 803
    Beta strandi81 – 888
    Beta strandi90 – 923
    Beta strandi94 – 10310
    Beta strandi108 – 1114
    Beta strandi112 – 1165
    Helixi121 – 13616
    Beta strandi149 – 1557
    Helixi156 – 1583
    Beta strandi160 – 1667
    Helixi170 – 18011
    Turni184 – 1863
    Beta strandi187 – 1959
    Beta strandi201 – 2044
    Beta strandi207 – 2104
    Turni211 – 2133
    Beta strandi214 – 2174
    Beta strandi220 – 2245
    Beta strandi227 – 2326
    Helixi234 – 2363
    Beta strandi242 – 2454
    Beta strandi248 – 25710
    Beta strandi259 – 2613
    Beta strandi263 – 2686
    Beta strandi272 – 2809
    Beta strandi283 – 2864
    Beta strandi298 – 3036
    Turni304 – 3063
    Beta strandi307 – 32216
    Beta strandi325 – 3339
    Beta strandi345 – 3473
    Beta strandi352 – 3609
    Beta strandi366 – 3683
    Helixi373 – 3753
    Beta strandi378 – 3825
    Helixi383 – 3908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BOQX-ray2.10A200-397[»]
    1GBAX-ray2.15A200-397[»]
    1GBBX-ray2.15A200-397[»]
    1GBCX-ray2.20A200-397[»]
    1GBDX-ray2.20A200-397[»]
    1GBEX-ray2.30A200-397[»]
    1GBFX-ray2.15A200-397[»]
    1GBHX-ray2.20A200-397[»]
    1GBIX-ray2.30A200-397[»]
    1GBJX-ray2.00A200-397[»]
    1GBKX-ray2.13A200-397[»]
    1GBLX-ray2.15A200-397[»]
    1GBMX-ray2.28A200-397[»]
    1P01X-ray2.00A200-397[»]
    1P02X-ray2.00A200-397[»]
    1P03X-ray2.15A200-397[»]
    1P04X-ray2.55A200-397[»]
    1P05X-ray2.10A200-397[»]
    1P06X-ray2.34A200-397[»]
    1P09X-ray2.20A200-397[»]
    1P10X-ray2.25A200-397[»]
    1P11X-ray1.93E200-397[»]
    1P12X-ray1.90E200-397[»]
    1QQ4X-ray1.20A200-397[»]
    1QRWX-ray1.20A200-397[»]
    1QRXX-ray1.60A200-397[»]
    1SSXX-ray0.83A200-397[»]
    1TALX-ray1.50A200-397[»]
    2ALPX-ray1.70A200-397[»]
    2H5CX-ray0.82A200-397[»]
    2H5DX-ray0.90A200-397[»]
    2LPRX-ray2.25A200-397[»]
    2PROX-ray3.00A/B/C34-199[»]
    2ULLX-ray1.50A200-397[»]
    3LPRX-ray2.15A200-397[»]
    3M7TX-ray1.55A200-397[»]
    3M7UX-ray1.05A200-397[»]
    3PROX-ray1.80A/B200-397[»]
    C/D34-199[»]
    3QGJX-ray1.30A/C200-397[»]
    3URCX-ray1.10A200-397[»]
    3URDX-ray1.08A200-397[»]
    3UREX-ray1.49A/B200-397[»]
    4PROX-ray2.40A/B200-397[»]
    C/D34-199[»]
    5LPRX-ray2.13A200-397[»]
    6LPRX-ray2.10A200-397[»]
    7LPRX-ray2.05A200-397[»]
    8LPRX-ray2.25A200-397[»]
    9LPRX-ray2.20A200-397[»]
    ProteinModelPortaliP00778.
    SMRiP00778. Positions 38-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00778.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR004236. Pept_S1_alpha_lytic.
    IPR001316. Pept_S1A_streptogrisin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF02983. Pro_Al_protease. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001134. Streptogrisin. 1 hit.
    PRINTSiPR00861. ALYTICPTASE.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00778-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG    50
    IFPTQLPQYL QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT 100
    SGARKSSTLG GVEVRNVRYS LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ 150
    SWYVDPRSNA VVVKVDDGAT EAGVDFVALS GADSAQVRIE SSPGKLQTTA 200
    NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN ATARIGGAVV 250
    GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC 300
    RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA 350
    GQAQGVMSGG NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG 397
    Length:397
    Mass (Da):41,077
    Last modified:February 1, 1996 - v3
    Checksum:i267FE6EBF57F33CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711E → D in AAA74111. (PubMed:3234766)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04052 Genomic DNA. Translation: AAA25409.1.
    M22763 Genomic DNA. Translation: AAA74111.1.
    PIRiA31772. TRYXB4.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04052 Genomic DNA. Translation: AAA25409.1 .
    M22763 Genomic DNA. Translation: AAA74111.1 .
    PIRi A31772. TRYXB4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BOQ X-ray 2.10 A 200-397 [» ]
    1GBA X-ray 2.15 A 200-397 [» ]
    1GBB X-ray 2.15 A 200-397 [» ]
    1GBC X-ray 2.20 A 200-397 [» ]
    1GBD X-ray 2.20 A 200-397 [» ]
    1GBE X-ray 2.30 A 200-397 [» ]
    1GBF X-ray 2.15 A 200-397 [» ]
    1GBH X-ray 2.20 A 200-397 [» ]
    1GBI X-ray 2.30 A 200-397 [» ]
    1GBJ X-ray 2.00 A 200-397 [» ]
    1GBK X-ray 2.13 A 200-397 [» ]
    1GBL X-ray 2.15 A 200-397 [» ]
    1GBM X-ray 2.28 A 200-397 [» ]
    1P01 X-ray 2.00 A 200-397 [» ]
    1P02 X-ray 2.00 A 200-397 [» ]
    1P03 X-ray 2.15 A 200-397 [» ]
    1P04 X-ray 2.55 A 200-397 [» ]
    1P05 X-ray 2.10 A 200-397 [» ]
    1P06 X-ray 2.34 A 200-397 [» ]
    1P09 X-ray 2.20 A 200-397 [» ]
    1P10 X-ray 2.25 A 200-397 [» ]
    1P11 X-ray 1.93 E 200-397 [» ]
    1P12 X-ray 1.90 E 200-397 [» ]
    1QQ4 X-ray 1.20 A 200-397 [» ]
    1QRW X-ray 1.20 A 200-397 [» ]
    1QRX X-ray 1.60 A 200-397 [» ]
    1SSX X-ray 0.83 A 200-397 [» ]
    1TAL X-ray 1.50 A 200-397 [» ]
    2ALP X-ray 1.70 A 200-397 [» ]
    2H5C X-ray 0.82 A 200-397 [» ]
    2H5D X-ray 0.90 A 200-397 [» ]
    2LPR X-ray 2.25 A 200-397 [» ]
    2PRO X-ray 3.00 A/B/C 34-199 [» ]
    2ULL X-ray 1.50 A 200-397 [» ]
    3LPR X-ray 2.15 A 200-397 [» ]
    3M7T X-ray 1.55 A 200-397 [» ]
    3M7U X-ray 1.05 A 200-397 [» ]
    3PRO X-ray 1.80 A/B 200-397 [» ]
    C/D 34-199 [» ]
    3QGJ X-ray 1.30 A/C 200-397 [» ]
    3URC X-ray 1.10 A 200-397 [» ]
    3URD X-ray 1.08 A 200-397 [» ]
    3URE X-ray 1.49 A/B 200-397 [» ]
    4PRO X-ray 2.40 A/B 200-397 [» ]
    C/D 34-199 [» ]
    5LPR X-ray 2.13 A 200-397 [» ]
    6LPR X-ray 2.10 A 200-397 [» ]
    7LPR X-ray 2.05 A 200-397 [» ]
    8LPR X-ray 2.25 A 200-397 [» ]
    9LPR X-ray 2.20 A 200-397 [» ]
    ProteinModelPortali P00778.
    SMRi P00778. Positions 38-397.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00778.

    Family and domain databases

    InterProi IPR004236. Pept_S1_alpha_lytic.
    IPR001316. Pept_S1A_streptogrisin.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF02983. Pro_Al_protease. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001134. Streptogrisin. 1 hit.
    PRINTSi PR00861. ALYTICPTASE.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes."
      Epstein D.M., Wensink P.C.
      J. Biol. Chem. 263:16586-16590(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
    2. Epstein D.M.
      Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme."
      Silen J.L., McGrath C.N., Smith K.R., Agard D.A.
      Gene 69:237-244(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
    4. "Priaary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases."
      Olson M.O.J., Nagabhushan N., Dzwiniel M., Smillie L.B., Whitaker D.R.
      Nature 228:438-442(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 199-396.
      Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
    5. "Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8-A resolution."
      Brayer G.D., Delbaere L.T.J., James M.N.G.
      J. Mol. Biol. 131:743-775(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    6. "Refined structure of alpha-lytic protease at 1.7-A resolution. Analysis of hydrogen bonding and solvent structure."
      Fujinaga M., Delbaere L.T.J., Brayer G.D., James M.N.G.
      J. Mol. Biol. 184:479-502(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    7. "Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of alpha-lytic protease."
      Peters R.J., Shiau A.K., Sohl J.L., Anderson D.E., Tang G., Silen J.L., Agard D.A.
      Biochemistry 37:12058-12067(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
      Strain: ATCC 29487 / DSM 2043 / LMG 8762 / UASM 495 / VKM B-2235.
    8. "Structure of alpha-lytic protease complexed with its pro region."
      Sauter N.K., Mau T., Rader S.D., Agard D.A.
      Nat. Struct. Biol. 5:945-950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiPRLA_LYSEN
    AccessioniPrimary (citable) accession number: P00778
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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