PRLA_LYSEN
ID PRLA_LYSEN Reviewed; 397 AA.
AC P00778;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-lytic protease;
DE EC=3.4.21.12;
DE AltName: Full=Alpha-lytic endopeptidase;
DE Flags: Precursor;
GN Name=alpha-LP;
OS Lysobacter enzymogenes.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29487 / DSM 2043 / BCRC 11654 / KCTC 12131 / LMG 8762 / VKM
RC B-2235 / UASM 495 / Ly e1;
RX PubMed=3053694; DOI=10.1016/s0021-9258(18)37430-1;
RA Epstein D.M., Wensink P.C.;
RT "The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide
RT sequence predicts a large prepro-peptide with homology to pro-peptides of
RT other chymotrypsin-like enzymes.";
RL J. Biol. Chem. 263:16586-16590(1988).
RN [2]
RP SEQUENCE REVISION.
RA Epstein D.M.;
RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29487 / DSM 2043 / BCRC 11654 / KCTC 12131 / LMG 8762 / VKM
RC B-2235 / UASM 495 / Ly e1;
RX PubMed=3234766; DOI=10.1016/0378-1119(88)90434-9;
RA Silen J.L., McGrath C.N., Smith K.R., Agard D.A.;
RT "Molecular analysis of the gene encoding alpha-lytic protease: evidence for
RT a preproenzyme.";
RL Gene 69:237-244(1988).
RN [4]
RP PROTEIN SEQUENCE OF 199-396.
RC STRAIN=ATCC 29487 / DSM 2043 / BCRC 11654 / KCTC 12131 / LMG 8762 / VKM
RC B-2235 / UASM 495 / Ly e1;
RX PubMed=5482494; DOI=10.1038/228438a0;
RA Olson M.O.J., Nagabhushan N., Dzwiniel M., Smillie L.B., Whitaker D.R.;
RT "Priaary structure of alpha-lytic protease: a bacterial homologue of the
RT pancreatic serine proteases.";
RL Nature 228:438-442(1970).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=117110; DOI=10.1016/0022-2836(79)90200-6;
RA Brayer G.D., Delbaere L.T.J., James M.N.G.;
RT "Molecular structure of the alpha-lytic protease from Myxobacter 495 at
RT 2.8-A resolution.";
RL J. Mol. Biol. 131:743-775(1979).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=3900416; DOI=10.1016/0022-2836(85)90296-7;
RA Fujinaga M., Delbaere L.T.J., Brayer G.D., James M.N.G.;
RT "Refined structure of alpha-lytic protease at 1.7-A resolution. Analysis of
RT hydrogen bonding and solvent structure.";
RL J. Mol. Biol. 184:479-502(1985).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=ATCC 29487 / DSM 2043 / BCRC 11654 / KCTC 12131 / LMG 8762 / VKM
RC B-2235 / UASM 495 / Ly e1;
RX PubMed=9724517; DOI=10.1021/bi980883v;
RA Peters R.J., Shiau A.K., Sohl J.L., Anderson D.E., Tang G., Silen J.L.,
RA Agard D.A.;
RT "Pro region C-terminus: protease active site interactions are critical in
RT catalyzing the folding of alpha-lytic protease.";
RL Biochemistry 37:12058-12067(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9808037; DOI=10.1038/2919;
RA Sauter N.K., Mau T., Rader S.D., Agard D.A.;
RT "Structure of alpha-lytic protease complexed with its pro region.";
RL Nat. Struct. Biol. 5:945-950(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell
CC walls, elastin and other proteins.; EC=3.4.21.12;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; J04052; AAA25409.1; -; Genomic_DNA.
DR EMBL; M22763; AAA74111.1; -; Genomic_DNA.
DR PIR; A31772; TRYXB4.
DR PDB; 1BOQ; X-ray; 2.10 A; A=200-397.
DR PDB; 1GBA; X-ray; 2.15 A; A=200-397.
DR PDB; 1GBB; X-ray; 2.15 A; A=200-397.
DR PDB; 1GBC; X-ray; 2.20 A; A=200-397.
DR PDB; 1GBD; X-ray; 2.20 A; A=200-397.
DR PDB; 1GBE; X-ray; 2.30 A; A=200-397.
DR PDB; 1GBF; X-ray; 2.15 A; A=200-397.
DR PDB; 1GBH; X-ray; 2.20 A; A=200-397.
DR PDB; 1GBI; X-ray; 2.30 A; A=200-397.
DR PDB; 1GBJ; X-ray; 2.00 A; A=200-397.
DR PDB; 1GBK; X-ray; 2.13 A; A=200-397.
DR PDB; 1GBL; X-ray; 2.15 A; A=200-397.
DR PDB; 1GBM; X-ray; 2.28 A; A=200-397.
DR PDB; 1P01; X-ray; 2.00 A; A=200-397.
DR PDB; 1P02; X-ray; 2.00 A; A=200-397.
DR PDB; 1P03; X-ray; 2.15 A; A=200-397.
DR PDB; 1P04; X-ray; 2.55 A; A=200-397.
DR PDB; 1P05; X-ray; 2.10 A; A=200-397.
DR PDB; 1P06; X-ray; 2.34 A; A=200-397.
DR PDB; 1P09; X-ray; 2.20 A; A=200-397.
DR PDB; 1P10; X-ray; 2.25 A; A=200-397.
DR PDB; 1P11; X-ray; 1.93 A; E=200-397.
DR PDB; 1P12; X-ray; 1.90 A; E=200-397.
DR PDB; 1QQ4; X-ray; 1.20 A; A=200-397.
DR PDB; 1QRW; X-ray; 1.20 A; A=200-397.
DR PDB; 1QRX; X-ray; 1.60 A; A=200-397.
DR PDB; 1SSX; X-ray; 0.83 A; A=200-397.
DR PDB; 1TAL; X-ray; 1.50 A; A=200-397.
DR PDB; 2ALP; X-ray; 1.70 A; A=200-397.
DR PDB; 2H5C; X-ray; 0.82 A; A=200-397.
DR PDB; 2H5D; X-ray; 0.90 A; A=200-397.
DR PDB; 2LPR; X-ray; 2.25 A; A=200-397.
DR PDB; 2PRO; X-ray; 3.00 A; A/B/C=34-199.
DR PDB; 2ULL; X-ray; 1.50 A; A=200-397.
DR PDB; 3LPR; X-ray; 2.15 A; A=200-397.
DR PDB; 3M7T; X-ray; 1.55 A; A=200-397.
DR PDB; 3M7U; X-ray; 1.05 A; A=200-397.
DR PDB; 3PRO; X-ray; 1.80 A; A/B=200-397, C/D=34-199.
DR PDB; 3QGJ; X-ray; 1.30 A; A/C=200-397.
DR PDB; 3URC; X-ray; 1.10 A; A=200-397.
DR PDB; 3URD; X-ray; 1.08 A; A=200-397.
DR PDB; 3URE; X-ray; 1.49 A; A/B=200-397.
DR PDB; 4PRO; X-ray; 2.40 A; A/B=200-397, C/D=34-199.
DR PDB; 5LPR; X-ray; 2.13 A; A=200-397.
DR PDB; 5WOT; NMR; -; A=200-397.
DR PDB; 6LPR; X-ray; 2.10 A; A=200-397.
DR PDB; 7LPR; X-ray; 2.05 A; A=200-397.
DR PDB; 8LPR; X-ray; 2.25 A; A=200-397.
DR PDB; 9LPR; X-ray; 2.20 A; A=200-397.
DR PDBsum; 1BOQ; -.
DR PDBsum; 1GBA; -.
DR PDBsum; 1GBB; -.
DR PDBsum; 1GBC; -.
DR PDBsum; 1GBD; -.
DR PDBsum; 1GBE; -.
DR PDBsum; 1GBF; -.
DR PDBsum; 1GBH; -.
DR PDBsum; 1GBI; -.
DR PDBsum; 1GBJ; -.
DR PDBsum; 1GBK; -.
DR PDBsum; 1GBL; -.
DR PDBsum; 1GBM; -.
DR PDBsum; 1P01; -.
DR PDBsum; 1P02; -.
DR PDBsum; 1P03; -.
DR PDBsum; 1P04; -.
DR PDBsum; 1P05; -.
DR PDBsum; 1P06; -.
DR PDBsum; 1P09; -.
DR PDBsum; 1P10; -.
DR PDBsum; 1P11; -.
DR PDBsum; 1P12; -.
DR PDBsum; 1QQ4; -.
DR PDBsum; 1QRW; -.
DR PDBsum; 1QRX; -.
DR PDBsum; 1SSX; -.
DR PDBsum; 1TAL; -.
DR PDBsum; 2ALP; -.
DR PDBsum; 2H5C; -.
DR PDBsum; 2H5D; -.
DR PDBsum; 2LPR; -.
DR PDBsum; 2PRO; -.
DR PDBsum; 2ULL; -.
DR PDBsum; 3LPR; -.
DR PDBsum; 3M7T; -.
DR PDBsum; 3M7U; -.
DR PDBsum; 3PRO; -.
DR PDBsum; 3QGJ; -.
DR PDBsum; 3URC; -.
DR PDBsum; 3URD; -.
DR PDBsum; 3URE; -.
DR PDBsum; 4PRO; -.
DR PDBsum; 5LPR; -.
DR PDBsum; 5WOT; -.
DR PDBsum; 6LPR; -.
DR PDBsum; 7LPR; -.
DR PDBsum; 8LPR; -.
DR PDBsum; 9LPR; -.
DR AlphaFoldDB; P00778; -.
DR BMRB; P00778; -.
DR SMR; P00778; -.
DR ChEMBL; CHEMBL3085615; -.
DR DrugBank; DB07411; PHENYLALANINE BORONIC ACID.
DR DrugBank; DB04237; Tris(Hydroxyethyl)Aminomethane.
DR MEROPS; S01.268; -.
DR KEGG; ag:AAA25409; -.
DR BRENDA; 3.4.21.12; 3118.
DR EvolutionaryTrace; P00778; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.300.50; -; 2.
DR InterPro; IPR037295; Alpha-lytic_protease_prodomain.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035070; Streptogrisin_prodomain.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001134; Streptogrisin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF54806; SSF54806; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..199
FT /id="PRO_0000026907"
FT CHAIN 200..397
FT /note="Alpha-lytic protease"
FT /id="PRO_0000026908"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 216..236
FT DISULFID 300..310
FT DISULFID 336..369
FT CONFLICT 171
FT /note="E -> D (in Ref. 3; AAA74111)"
FT /evidence="ECO:0000305"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 56..77
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4PRO"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4PRO"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3PRO"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:3PRO"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3PRO"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2H5C"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2H5C"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2H5C"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 307..322
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2H5C"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:2H5C"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2H5C"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:2H5C"
SQ SEQUENCE 397 AA; 41077 MW; 267FE6EBF57F33CB CRC64;
MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG IFPTQLPQYL
QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT SGARKSSTLG GVEVRNVRYS
LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ SWYVDPRSNA VVVKVDDGAT EAGVDFVALS
GADSAQVRIE SSPGKLQTTA NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN
ATARIGGAVV GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC
RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA GQAQGVMSGG
NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG
