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P00778

- PRLA_LYSEN

UniProt

P00778 - PRLA_LYSEN

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Protein
Alpha-lytic protease
Gene
alpha-LP
Organism
Lysobacter enzymogenes
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 system By similarity
Active sitei262 – 2621Charge relay system By similarity
Active sitei342 – 3421Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed prediction
Add
BLAST
Propeptidei25 – 199175
PRO_0000026907Add
BLAST
Chaini200 – 397198Alpha-lytic protease
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP00778.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S1 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711E → D in AAA74111. 1 Publication

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: May 14, 2014
This is version 107 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

Similar proteinsi