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Database: UniProt
Entry: Q84DL9_LISWE
LinkDB: Q84DL9_LISWE
Original site: Q84DL9_LISWE 
ID   Q84DL9_LISWE            Unreviewed;       522 AA.
AC   Q84DL9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   28-JUN-2023, entry version 62.
DE   RecName: Full=Probable endopeptidase p60 {ECO:0000256|ARBA:ARBA00013385};
DE   AltName: Full=Invasion-associated protein p60 {ECO:0000256|ARBA:ARBA00032855};
GN   Name=iap {ECO:0000313|EMBL:AAO83983.1};
OS   Listeria welshimeri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1643 {ECO:0000313|EMBL:AAO83983.1};
RN   [1] {ECO:0000313|EMBL:AAO83983.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TUMLis35 {ECO:0000313|EMBL:AAO83983.1};
RA   Schmid M.W., Walcher M., Bubert A., Wagner M., Schleifer K.-H.;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAO83983.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TUMLis35 {ECO:0000313|EMBL:AAO83983.1};
RX   PubMed=12648840; DOI=10.1016/S0928-8244(02)00456-X;
RA   Schmid M., Walcher M., Bubert A., Wagner M., Wagner M., Schleifer K.-H.;
RT   "Nucleic acid-based, cultivation-independent detection of Listeria spp and
RT   genotypes of L monocytogenes.";
RL   FEMS Immunol. Med. Microbiol. 35:215-225(2003).
CC   -!- FUNCTION: This major extracellular protein may be involved in the
CC       invasion of non-professional phagocytic cells by Listeria.
CC       {ECO:0000256|ARBA:ARBA00003740}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family.
CC       {ECO:0000256|ARBA:ARBA00007074}.
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DR   EMBL; AF532301; AAO83983.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84DL9; -.
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; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 3.10.350.10; LysM domain; 3.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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   PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
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; Cysteine proteinases; 1.
DR   SUPFAM; SSF54106; LysM domain; 3.
DR   PROSITE; PS51782; LYSM; 3.
DR   PROSITE; PS51935; NLPC_P60; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..522
FT                   /note="Probable endopeptidase p60"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039074326"
FT   DOMAIN          28..71
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          78..142
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          196..239
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          314..357
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          404..522
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          154..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  53956 MW;  FD406804620E1E3E CRC64;
     MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD ALKKANNLTS
     DKIVPGQKLQ VTEVASEKTE KSVSATWLNV RSGAGVDNSI VTSLKGGTKV TVEAAESNGW
     NKISYGEGKT GYVNGKYLGD AVTSAPVAKQ EVKQETTKQT VPAAETKTEV KQSTPAPTAP
     KAAETKTAPV VDTNATTHTV KSGDTIWALS VKYGASVQDL MSWNNLSSSS IYVGQKIAVK
     QSAAKTAAPK AEVKTEAPAV EKETSTPVVK ENTNTTVKKE VTTQTQTNTT KAPAQAAKPA
     PAPAPAPTVN TNASTYTVKS GDSLSKIANT FGTSVSKIKA LNNLTSDNLQ VGTVLKVKGT
     VPTTNTNNNS NTTAPTTNTS NNNTSSNTST PSKNTNTNTN QGSSNSASAL IAEAQKHLGK
     AYSWGGNGPT TFDCSGFTSY VFAKSGISLP RTSGAQYAST SRISESQAKP GDLVFFDYGS
     GIAHVGIYVG NGQMINAQDN GVKYDNIHGS GWGKYLVGFG RV
//
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