ID   P60_LISGR               Reviewed;         511 AA.
AC   Q01835;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 89.
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 grayi (Listeria murrayi).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1641;
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; M80352; AAA25285.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01835; -.
DR   SMR; Q01835; -.
DR   PRIDE; Q01835; -.
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..511
FT                   /note="Probable endopeptidase p60"
FT                   /id="PRO_0000019757"
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          175..218
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          297..341
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          393..511
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          229..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        423
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        473
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        485
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   511 AA;  53181 MW;  2FD0ED174E3810D0 CRC64;
     MNMKKATIVS AAGIAVTAFA APSVVSANTV VVASGDTLWG IASKTGTTVD QLKQLNKLDS
     DRIVPGQKLT IKEVAAQKVE KSVSATWLNV RHAPDANEKI LTSLKGRTVV KVESSEANGW
     NKISFDNGKT GYVNGKYLSD AKVAAPVVTK AVTHKAEAKV AATSTHAVKV DTNASTYKVK
     SGDTIWALSV KYGVPVQKLI EWNNLSSSSI YVGQTIAVKE AAAKAAPTTV KQAAPAKVAP
     KQEVKQTAPA KQEQAKPAAK ETVKPAVSKP KAATPAPTAK PAVEQKASTP AVDTNAATYK
     VQNGDSLGKI ASLFKVSVAD LTNWNNLNAT ITIYAGQELS VKASAAKPKP AAPAKPAVSK
     PATSTPAKVT PTNTTNNSTP TTNVNNNTSQ SSSASFSALY AEAKKHLGKP YTWGARGPST
     FDCSGFTSYV FNQVGLSLSG NSATQYANST KISESQAQPG DLVFFNYGSG IAHVGIYIGG
     GQMIDAQDNG VSIDNIHGNG WGQYLVGFGR V