ID A0A0K9YQQ0_9BACL Unreviewed; 301 AA.
AC A0A0K9YQQ0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable endopeptidase p60 {ECO:0000256|ARBA:ARBA00013385};
DE AltName: Full=Invasion-associated protein p60 {ECO:0000256|ARBA:ARBA00032855};
GN ORFNames=ADS79_19245 {ECO:0000313|EMBL:KNB70967.1};
OS Brevibacillus reuszeri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54915 {ECO:0000313|EMBL:KNB70967.1, ECO:0000313|Proteomes:UP000036834};
RN [1] {ECO:0000313|Proteomes:UP000036834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9887 {ECO:0000313|Proteomes:UP000036834};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNB70967.1}.
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DR EMBL; LGIQ01000009; KNB70967.1; -; Genomic_DNA.
DR RefSeq; WP_049739999.1; NZ_LGIQ01000009.1.
DR AlphaFoldDB; A0A0K9YQQ0; -.
DR STRING; 54915.ADS79_19245; -.
DR PATRIC; fig|54915.3.peg.2950; -.
DR OrthoDB; 9813368at2; -.
DR Proteomes; UP000036834; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
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; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KNB70967.1};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..301
FT /note="Probable endopeptidase p60"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005533646"
FT DOMAIN 26..69
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 103..165
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 177..301
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 301 AA; 32468 MW; 79719624345D3BAD CRC64;
MKHTSKVFTL LALFTLLPTA AHAASPAYVV SAGDTLSKIA RENHTTVDQL IQVNQLHTDQ
LSIGQTLSLP TTGLSDSVDE AAPPDVIEGN NQSHSESEGI TAGEKARVTG DVLNVRKKPS
TDAKILGKLK FGSLVEVLET GSEWTKIEFE DDEAYVATEF LSAKLSSLPV MSGDIDSASL
GRLESIFTPL LKTPYVLGGT TPNGFDCSGF TSYVFNQLGV TLPRTSEDQF NGGQAVSLDE
AQPGDLLFYD ALGKGRVSHV AIYLGNGTIV HANGDDVRYG KVEYMHKLYP FYGAKRYIQF
Q
//
