ID W2EBC4_9BACL Unreviewed; 348 AA.
AC W2EBC4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=NlpC/P60 domain-containing protein {ECO:0000259|PROSITE:PS51935};
GN ORFNames=ERIC1_1c18380 {ECO:0000313|EMBL:ETK28376.1};
OS Paenibacillus larvae subsp. larvae DSM 25719.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697286 {ECO:0000313|EMBL:ETK28376.1, ECO:0000313|Proteomes:UP000018834};
RN [1] {ECO:0000313|EMBL:ETK28376.1, ECO:0000313|Proteomes:UP000018834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25719 {ECO:0000313|EMBL:ETK28376.1,
RC ECO:0000313|Proteomes:UP000018834};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
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:ETK28376.1}.
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DR EMBL; ADFW01000001; ETK28376.1; -; Genomic_DNA.
DR RefSeq; WP_051427933.1; NZ_ADFW01000001.1.
DR AlphaFoldDB; W2EBC4; -.
DR PATRIC; fig|697286.3.peg.1977; -.
DR OrthoDB; 9813118at2; -.
DR Proteomes; UP000018834; Unassembled WGS sequence.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_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; PF07833; Cu_amine_oxidN1; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..348
FT /note="NlpC/P60 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004815779"
FT DOMAIN 231..348
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 167..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 37552 MW; 3EA9FD3EBF774E02 CRC64;
MATKWLKSLV LSGTLVTVGL IASNTTAHAA IPDGVKVQIN NHLVNFSDAM PYLNQGSIMV
PLRAVAENLG YKLEFEMIQN GTQVRVKLIG DGHVFEFESG KQEAKVDNRS ITLDEAPVIK
NDRVYVHIRS IGEHFGHIVQ WDMNNNIGIL GADGKYHAPA WYKPAKRTTP SKDVTLSAKK
SNESAGKQHT GKPADKQVSS AKKANESAGK QHTEKSADKK VEPATSKEIA STDKKSIVSK
ATGQVGVPYL WGGSSPSGFD CSGLVTYIFK QQGINLPRTS SGMYGVGTSV SNPEQGDLVF
FANGGKVFHV GVYVGGNRFI SATDDGVKID SLGNSYWNKY YIGAKKVM
//
