Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00778

- PRLA_LYSEN

UniProt

P00778 - PRLA_LYSEN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 systemBy similarity
Active sitei262 – 2621Charge relay systemBy similarity
Active sitei342 – 3421Charge relay systemBy 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 – 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 – 4910Combined sources
Helixi53 – 553Combined sources
Helixi56 – 7722Combined sources
Helixi78 – 803Combined sources
Beta strandi81 – 888Combined sources
Beta strandi90 – 923Combined sources
Beta strandi94 – 10310Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi112 – 1165Combined sources
Helixi121 – 13616Combined sources
Beta strandi149 – 1557Combined sources
Helixi156 – 1583Combined sources
Beta strandi160 – 1667Combined sources
Helixi170 – 18011Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1959Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi207 – 2104Combined sources
Turni211 – 2133Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi227 – 2326Combined sources
Helixi234 – 2363Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi248 – 25710Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi272 – 2809Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi298 – 3036Combined sources
Turni304 – 3063Combined sources
Beta strandi307 – 32216Combined sources
Beta strandi325 – 3339Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi352 – 3609Combined sources
Beta strandi366 – 3683Combined sources
Helixi373 – 3753Combined sources
Beta strandi378 – 3825Combined sources
Helixi383 – 3908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG
60 70 80 90 100
IFPTQLPQYL QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT
110 120 130 140 150
SGARKSSTLG GVEVRNVRYS LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ
160 170 180 190 200
SWYVDPRSNA VVVKVDDGAT EAGVDFVALS GADSAQVRIE SSPGKLQTTA
210 220 230 240 250
NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN ATARIGGAVV
260 270 280 290 300
GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC
310 320 330 340 350
RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA
360 370 380 390
GQAQGVMSGG NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG
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:
EMBLi
GenBanki
DDBJi
Links Updated
J04052 Genomic DNA. Translation: AAA25409.1.
M22763 Genomic DNA. Translation: AAA74111.1.
PIRiA31772. TRYXB4.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04052 Genomic DNA. Translation: AAA25409.1 .
M22763 Genomic DNA. Translation: AAA74111.1 .
PIRi A31772. TRYXB4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

ChEMBLi CHEMBL3085615.

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: November 26, 2014
This is version 110 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