ID M8DB07_9BACL Unreviewed; 307 AA.
AC M8DB07;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Probable endopeptidase p60 {ECO:0000256|ARBA:ARBA00013385};
DE AltName: Full=Invasion-associated protein p60 {ECO:0000256|ARBA:ARBA00032855};
GN ORFNames=I532_05685 {ECO:0000313|EMBL:EMT53479.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT53479.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT53479.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT53479.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) 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:EMT53479.1}.
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DR EMBL; APBN01000002; EMT53479.1; -; Genomic_DNA.
DR RefSeq; WP_003386952.1; NZ_APBN01000002.1.
DR AlphaFoldDB; M8DB07; -.
DR STRING; 1300222.I532_05685; -.
DR GeneID; 72734298; -.
DR PATRIC; fig|1300222.3.peg.1167; -.
DR OrthoDB; 9813368at2; -.
DR Proteomes; UP000012081; 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 SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000012081};
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..307
FT /note="Probable endopeptidase p60"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004095178"
FT DOMAIN 26..69
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 184..305
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 307 AA; 33265 MW; 0352800ACE8CE9B9 CRC64;
MKKTTRILAI LSVCAFMPVT AHASSPVYVV QAGDTLMKIA RENQTTVQEL MQVNQLSSDR
LSIGQSLSLP GTATPPVYAA AESAVNEAPA DIVSQGKSSS IRAGIKARIT GDIVNVRKSP
TLDSEVIGKL PMGAVVDVLD PGAEWTKISF GQDESFVATD YLDEVSSSSE SSSKEESKKR
KKSSFSTKEL YRAFEPLLNT PYVLGGTTTS GFDCSGFTSY VFKELGITLP RTSEEQFQGG
QAVSLDDALP GDLVFYDTMG RGRVSHVAIY LGDDLIVHAN GDDVRYEKLS NMHKLYPFFG
VKRYSDE
//
