ID   P60_LISWE               Reviewed;         524 AA.
AC   Q01839;
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 welshimeri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1643;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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; M80354; AAA25287.1; -; Genomic_DNA.
DR   EMBL; M80348; AAA25281.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q01839; -.
DR   SMR; Q01839; -.
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..524
FT                   /note="Probable endopeptidase p60"
FT                   /id="PRO_0000019762"
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          196..239
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          314..357
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          406..524
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          150..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        436
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        486
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   524 AA;  54086 MW;  22EAFE5DC4A254C9 CRC64;
     MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD ALKKANNLTS
     DKIVPGQKLQ VTEVASEKTE KSVSATWLNV RSGAGVDNSI VTSLKGGTKV TVEAAESNGW
     NKISYGEGKT GYVNGKYLGD AVTSAPVAKQ EVKQETTKQT APAAETKTEV KQSTPAPTAP
     KAAETKTAPV VDTNATTHTV KSGDTIWALS VKYGASVQDL MSWNNLSSSS IYVGQKIAVK
     QSAAKTAAPK AEVKTEAPAV EKETSTPVVK ENTNTTVKKE VTTQTQTNTT KAPAQAAKPA
     PAPAPAPTVN TNASTYTVKS GDSLSKIANT FGTSVSKIKA LNNLTSDNLQ VGTVLKVKGT
     VPTTNTNNNS NTTAPTTNTS NNNTSSNTST PSKNTNTNTN QGSSNSASAS ALIAEAQKHL
     GKAYSWGGNG PTTFDCSGFT SYVFAKSGIS LPRTSGAQYA STSRISESQA KPGDLVFFDY
     GSGIAHVGIY VGNGQMINAQ DNGVKYDNIH GSGWGKYLVG FGRV