ID   P60_LISIV               Reviewed;         524 AA.
AC   Q01837;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
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 ivanovii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1638;
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; M80350; AAA25284.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01837; -.
DR   SMR; Q01837; -.
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_0000019759"
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          312..355
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          145..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..295
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;  54159 MW;  E22D579429817144 CRC64;
     MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQDKGTTVD ALKKANNLTS
     DKIVPGQKLQ ITEVASEKTE KSVTATWLNV RSGAGVDNSI VTSLKGGTKV TVESTEANGW
     YKISYGEGKT GYVNGKYLGT TVTSAPAPEV KEETTTQAQA APAAETKPEV KQSTPATVLP
     KAETKTETPA VDTTASTYTV KSGDTIWALS SKYGTSVQNI MSWNNLSSSS IYVGQVLAVK
     QEAAKTASPK AEVKTEAPTA EKQVSAPVVK ENTQTTTAKK EVTPQKQTNT QAPAQAAKPA
     PAPAPTVNTN ASSYTVKSGD TLSKIATTFG TTVSKIKALN GLNSDNLQVG QVLKVKGTVP
     TANTNSNSNA TAPTTNTNNN TSNTSTSTPS KNTNTNSNAS QGSSSTASAS SLIAEAQKHL
     GKAYSWGGNG PTTFDCSGFT KYVFAKSGVT LPRTSGAQYA SSTKISESQA KPGDLVFFDY
     GNGIAHVGIY VGNGQMINAQ DNGVKYDNIH GSGWGQFLVG FGRV