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Database: UniProt
Entry: A0A2B2BT70_9BACI
LinkDB: A0A2B2BT70_9BACI
Original site: A0A2B2BT70_9BACI 
ID   A0A2B2BT70_9BACI        Unreviewed;       257 AA.
AC   A0A2B2BT70;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidoglycan endopeptidase {ECO:0000313|EMBL:PFP25763.1};
GN   ORFNames=COJ96_18550 {ECO:0000313|EMBL:PFP25763.1};
OS   Bacillus sp. AFS073361.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP25763.1, ECO:0000313|Proteomes:UP000223997};
RN   [1] {ECO:0000313|EMBL:PFP25763.1, ECO:0000313|Proteomes:UP000223997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS073361 {ECO:0000313|EMBL:PFP25763.1,
RC   ECO:0000313|Proteomes:UP000223997};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PFP25763.1}.
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DR   EMBL; NUZU01000037; PFP25763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B2BT70; -.
DR   OrthoDB; 9813368at2; -.
DR   Proteomes; UP000223997; Unassembled WGS sequence.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
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   PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000223997};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..257
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012383020"
FT   DOMAIN          28..71
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          82..125
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          139..257
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
SQ   SEQUENCE   257 AA;  27675 MW;  9BEF7F5C3626D7EB CRC64;
     MKKHLLSIAA TAGILFSTYA GTASAHENIY TVQSGDTLWK ISQANKVTVA DLKIWNHLTS
     DSLNVNQKLT LLAPHSHETA TISYTVQKGD TLYLIASRNK LSVAQLKSLN NLTTDTIYVG
     QVLKLTTSGI STPVPAPTVS KAQMVMDEAK KYIGTPYLWG GNTPAGFDCS GLTSYVFNKV
     GVSIPRTAAT QWSGMKSVST PKPGDLVFFE TYAPGPTHVG IYLGNNQFIQ AGSKGVSIAD
     MTNSYWKPKY LGARTAF
//
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