P00778 (PRLA_LYSEN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-lytic protease
EC=3.4.21.12

Alternative name(s):
Alpha-lytic endopeptidase

Gene names

Name:

alpha-LP

Organism

Lysobacter enzymogenes

Taxonomic identifier

69 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.
Sequence similarities	Belongs to the peptidase S1 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Propeptide

25 – 199

175

PRO_0000026907

Chain

200 – 397

198

Alpha-lytic protease

PRO_0000026908

Sites

Active site

235

1

Charge relay system By similarity

Active site

262

1

Charge relay system By similarity

Active site

342

1

Charge relay system By similarity

Amino acid modifications

Disulfide bond

216 ↔ 236

Disulfide bond

300 ↔ 310

Disulfide bond

336 ↔ 369

Experimental info

Sequence conflict

171

1

E → D in AAA74111. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

397

Helix Strand Turn

Details...

Helix

40 – 47

8

Beta strand

53 – 56

4

Helix

57 – 77

21

Beta strand

80 – 88

9

Beta strand

94 – 102

9

Beta strand

108 – 111

4

Beta strand

113 – 116

4

Helix

121 – 133

13

Beta strand

152 – 155

4

Helix

156 – 158

3

Beta strand

160 – 164

5

Helix

170 – 180

11

Helix

184 – 186

3

Beta strand

201 – 204

4

Beta strand

207 – 210

4

Turn

211 – 213

3

Beta strand

214 – 217

4

Beta strand

220 – 224

5

Beta strand

227 – 232

6

Helix

234 – 236

3

Beta strand

242 – 245

4

Beta strand

248 – 257

10

Beta strand

259 – 261

3

Beta strand

263 – 268

6

Beta strand

272 – 280

9

Beta strand

283 – 286

4

Beta strand

298 – 303

6

Turn

304 – 306

3

Beta strand

307 – 322

16

Beta strand

325 – 333

9

Beta strand

345 – 347

3

Beta strand

352 – 360

9

Beta strand

366 – 368

3

Helix

373 – 375

3

Beta strand

378 – 382

5

Helix

383 – 390

8

Sequences

	Sequence		Length	Mass (Da)
	P00778 [UniParc]. Last modified February 1, 1996. Version 3. Checksum: 267FE6EBF57F33CB	FASTA	397	41,077
	10 20 30 40 50 60 MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG IFPTQLPQYL 70 80 90 100 110 120 QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT SGARKSSTLG GVEVRNVRYS 130 140 150 160 170 180 LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ SWYVDPRSNA VVVKVDDGAT EAGVDFVALS 190 200 210 220 230 240 GADSAQVRIE SSPGKLQTTA NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN 250 260 270 280 290 300 ATARIGGAVV GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC 310 320 330 340 350 360 RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA GQAQGVMSGG 370 380 390 NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG

References

[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04052 Genomic DNA. Translation: AAA25409.1.
M22763 Genomic DNA. Translation: AAA74111.1.

PIR

TRYXB4. A31772.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00778.

SMR

P00778. Positions 38-397.

ModBase

Search...

Protein family/group databases

MEROPS

S01.268.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR004236. Pept_S1_alpha_lytic.
IPR001316. Pept_S1A_streptogrisin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF02983. Pro_Al_protease. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001134. Streptogrisin. 1 hit.

PRINTS

PR00861. ALYTICPTASE.

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00778.

Entry information

Entry name

PRLA_LYSEN

Accession

Primary (citable) accession number: P00778

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program