ID Q84DU6_LISWE Unreviewed; 524 AA.
AC Q84DU6;
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:AAO83900.1};
OS Listeria welshimeri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1643 {ECO:0000313|EMBL:AAO83900.1};
RN [1] {ECO:0000313|EMBL:AAO83900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMVW1659 {ECO:0000313|EMBL:AAO83900.1};
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:AAO83900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMVW1659 {ECO:0000313|EMBL:AAO83900.1};
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; AF532218; AAO83900.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84DU6; -.
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..524
FT /note="Probable endopeptidase p60"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038594144"
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 406..524
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 151..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..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 151..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 54004 MW; 97CDF1CB0ED34F7E CRC64;
MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD ALKKANNLTS
DKIVPGQKLQ VTEVASEKTE KSVSATWLNV RSGAGVDNSI VTSLKGGTKV TVEAAESNGW
NKISYGEGKT GYVNGKYLGD ALTSAPVAKQ EVKQETTKQT APAAETKTEV KQSTPAPTAP
KAAETKTAPV VDTNATTHTV KSGDTMWALS VKYGASVQDL MSWNNLSSSS IYVGQKIAVK
QSAAKTAAPK AEVKTEAPAV EKETSTPVVK ENTNTTVKKE VTTQTQTNTT KAPAQAAKPA
PAPAPAPTVN TNASTYTVKS GDSLSKIANT FGTSVSKIKA LNNLTSDNLQ VGTVLKVKGT
VPTTNTNNNS NTTAPTTNTS NNNTSSNTST PSKNTNTNTN QGSSNSASAS ALIAEAQKHL
GKAYSWGGNG PTTFDCSGFA SYVFAKSGIS LPRTSGAQYA STSRVSESQA KPGDLVFFDY
GSGIAHVGIY VGDGQMINAQ DNGVGYDNIH GSGWGKYLVG FGRV
//
