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Protein

Alpha-lytic protease

Gene

alpha-LP

Organism
Lysobacter enzymogenes
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei235Charge relay systemBy similarity1
Active sitei262Charge relay systemBy similarity1
Active sitei342Charge relay systemBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.12 3118

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3085615
DrugBankiDB07411 PHENYLALANINE BORONIC ACID
DB04237 Tris(Hydroxyethyl)Aminomethane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002690725 – 199Add BLAST175
ChainiPRO_0000026908200 – 397Alpha-lytic proteaseAdd BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi216 ↔ 236
Disulfide bondi300 ↔ 310
Disulfide bondi336 ↔ 369

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP00778

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 49Combined sources10
Helixi53 – 55Combined sources3
Helixi56 – 77Combined sources22
Helixi78 – 80Combined sources3
Beta strandi81 – 88Combined sources8
Beta strandi90 – 92Combined sources3
Beta strandi94 – 103Combined sources10
Beta strandi108 – 111Combined sources4
Beta strandi112 – 116Combined sources5
Helixi121 – 136Combined sources16
Beta strandi149 – 155Combined sources7
Helixi156 – 158Combined sources3
Beta strandi160 – 166Combined sources7
Helixi170 – 180Combined sources11
Turni184 – 186Combined sources3
Beta strandi187 – 195Combined sources9
Beta strandi201 – 204Combined sources4
Beta strandi207 – 210Combined sources4
Turni211 – 213Combined sources3
Beta strandi214 – 217Combined sources4
Beta strandi220 – 224Combined sources5
Beta strandi227 – 232Combined sources6
Helixi234 – 236Combined sources3
Beta strandi242 – 245Combined sources4
Beta strandi248 – 257Combined sources10
Beta strandi259 – 261Combined sources3
Beta strandi263 – 268Combined sources6
Beta strandi272 – 280Combined sources9
Beta strandi283 – 286Combined sources4
Beta strandi298 – 303Combined sources6
Turni304 – 306Combined sources3
Beta strandi307 – 322Combined sources16
Beta strandi325 – 333Combined sources9
Beta strandi345 – 347Combined sources3
Beta strandi352 – 360Combined sources9
Beta strandi366 – 368Combined sources3
Helixi373 – 375Combined sources3
Beta strandi378 – 382Combined sources5
Helixi383 – 390Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5WOTNMR-A200-397[»]
6LPRX-ray2.10A200-397[»]
7LPRX-ray2.05A200-397[»]
8LPRX-ray2.25A200-397[»]
9LPRX-ray2.20A200-397[»]
ProteinModelPortaliP00778
SMRiP00778
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00778

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK20136

Family and domain databases

Gene3Di3.30.300.50, 2 hits
InterProiView protein in InterPro
IPR037295 Alpha-lytic_protease_prodomain
IPR004236 Pept_S1_alpha_lytic
IPR001316 Pept_S1A_streptogrisin
IPR009003 Peptidase_S1_PA
IPR035070 Streptogrisin_prodomain
IPR001254 Trypsin_dom
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF02983 Pro_Al_protease, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001134 Streptogrisin, 1 hit
PRINTSiPR00861 ALYTICPTASE
SUPFAMiSSF50494 SSF50494, 1 hit
SSF54806 SSF54806, 2 hits
PROSITEiView protein in PROSITE
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti171E → D in AAA74111 (PubMed:3234766).Curated1

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

Genome annotation databases

KEGGiag:AAA25409

Similar proteinsi

Entry informationi

Entry nameiPRLA_LYSEN
AccessioniPrimary (citable) accession number: P00778
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: May 23, 2018
This is version 124 of the entry and version 3 of the sequence. See 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

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