ID   P60_LISSE               Reviewed;         523 AA.
AC   Q01838;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable endopeptidase p60;
DE            EC=3.4.-.-;
DE   AltName: Full=Invasion-associated protein p60;
DE   Flags: Precursor;
GN   Name=iap;
OS   Listeria seeligeri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1514809; DOI=10.1128/aem.58.8.2625-2632.1992;
RA   Bubert A., Koehler S., Goebel W.;
RT   "The homologous and heterologous regions within the iap gene allow
RT   genus- and species-specific identification of Listeria spp. by polymerase
RT   chain reaction.";
RL   Appl. Environ. Microbiol. 58:2625-2632(1992).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=1459966; DOI=10.1128/jb.174.24.8166-8171.1992;
RA   Bubert A., Kuhn M., Goebel W., Koehler S.;
RT   "Structural and functional properties of the p60 proteins from different
RT   Listeria species.";
RL   J. Bacteriol. 174:8166-8171(1992).
CC   -!- FUNCTION: This major extracellular protein may be involved in the
CC       invasion of non-professional phagocytic cells by Listeria.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
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DR   EMBL; M80353; AAA25286.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01838; -.
DR   SMR; Q01838; -.
DR   STRING; 683837.lse_0492; -.
DR   eggNOG; COG0791; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3103; Bacteria.
DR   OMA; WIPELYL; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 3.
DR   Gene3D; 3.10.350.10; -; 3.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   Pfam; PF01476; LysM; 3.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   Pfam; PF08239; SH3_3; 1.
DR   SMART; SM00257; LysM; 3.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54106; SSF54106; 3.
DR   PROSITE; PS51782; LYSM; 3.
DR   PROSITE; PS51935; NLPC_P60; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Repeat; Signal; Thiol protease.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..523
FT                   /note="Probable endopeptidase p60"
FT                   /id="PRO_0000019761"
FT   DOMAIN          28..71
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          78..142
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   DOMAIN          198..241
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          318..361
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          405..523
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          146..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        485
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        497
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   523 AA;  53845 MW;  89341210D20DF6B4 CRC64;
     MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQDNGTTVD ALKKANKLTT
     DKIVPGQKLQ VTEVASEKTE KSVSATWLNV RSGAGVDNSI VTSLKGGTKV TVESTEANGW
     NKITYGEGKT GYVNGKYLGN AVTSAPSATP EVKQEETTQA APAQQTKTEV KQATPAATTE
     KDAVETKTTA PAVDTNATTH TVKSGDTIWA LSVKYGASVQ DLMSWNNLSS SSIYVGQNIA
     VKQSAAKNTA PKAEAKTEAP AAEKQTAAPV VKESTNTSTT TTVKKETTTE KQTSTTKAPA
     QAAKPAPAPA PTVNTNASSY TVKSGDTLGK IASTFGTTVS KIKALNGLTS DNLQVGDVLK
     VKGTVPATNT NTATAPTTNT NNNTSSSNTS TPSKNNNTNQ SSSNSSSASA IIAEAQKHLG
     KAYSWGGNGP TTFDCSGFTS YVFAQSGITL PRTSGAQYAS TTKVSESEAQ PGDLVFFDYG
     SGIAHVGIYV GNGQMINAQD NGVKYDNIHG SGWGQYLVGF GRV