PROA_LEGPN
ID PROA_LEGPN Reviewed; 543 AA.
AC P21347;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zinc metalloproteinase;
DE EC=3.4.24.-;
DE AltName: Full=PEP1;
DE AltName: Full=PRO A;
DE Flags: Precursor;
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 208-217.
RX PubMed=2110146; DOI=10.1128/jb.172.5.2608-2613.1990;
RA Black W.J., Quinn F.D., Tompkins L.S.;
RT "Legionella pneumophila zinc metalloprotease is structurally and
RT functionally homologous to Pseudomonas aeruginosa elastase.";
RL J. Bacteriol. 172:2608-2613(1990).
CC -!- FUNCTION: Cleaves collagen, gelatin, casein, alpha-1-antitrypsin, and
CC bovine insulin. May play a role in the pathogenesis of legionnaires
CC disease.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; M31884; AAA25301.1; -; Genomic_DNA.
DR PIR; A35265; A35265.
DR PDB; 6YA1; X-ray; 1.48 A; A=208-543.
DR PDB; 6YZE; X-ray; 2.18 A; A=208-543.
DR PDBsum; 6YA1; -.
DR PDBsum; 6YZE; -.
DR AlphaFoldDB; P21347; -.
DR SMR; P21347; -.
DR STRING; 91892.BIZ52_02605; -.
DR MEROPS; M04.006; -.
DR eggNOG; COG3227; Bacteria.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..207
FT /evidence="ECO:0000269|PubMed:2110146"
FT /id="PRO_0000028638"
FT CHAIN 208..543
FT /note="Zinc metalloproteinase"
FT /id="PRO_0000028639"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:6YA1"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:6YA1"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6YZE"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6YZE"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 303..322
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:6YA1"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 394..416
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6YA1"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:6YA1"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 484..497
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 505..519
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 523..532
FT /evidence="ECO:0007829|PDB:6YA1"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:6YA1"
SQ SEQUENCE 543 AA; 60704 MW; B811DDC591B92D6B CRC64;
MHPNYYLSPL AVAIALGIAS PVKAADPIPL QKSSFSEVTQ KFQLTLPGVM KGAVVSTNSL
QFIRQHTDGN KVTHVRMQQQ YAGFPVFGGY AILHSKNATP SLATAKSDEK MNGVIYDGLQ
AELGQPKPSF VKNASMALQQ FKDKYANKQV SEDQVTPMIY IDEKHQAHWA YKVSVLVIHD
DRIPERPTAI IDAETNKPFV QWDDVKTEKV QAKGMGFGGN RKIGEYQFGK DLPLLEITRD
SSVEMCFMEN TDVKVVDMGH KYYSNNKPMQ FTCKETPDTQ STKTYYTGYS ADGYDRDNGA
ASPTNDALYA GYVIKHMYHD WYGVEALTKS DGSPMQLVMR VHYGQGYENA YWDGKQMTFG
DGDTMMYPLV SLGVGGHEVS HGFTEQHSGL EYFGQSGGMN ESFSDMAAQA AEYYSVGKNS
WQIGPEIMKE DSGYDALRYM DKPSRDGMSI DVADDYYGGL DVHYSSGVYN HLFYILANQP
NWNLRMAFDV MVKANMDYWT PYSTFDEGGC GMLSAAKDLG YNLDDIKKSL SEVTINYQSC
YVD
