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Database: UniProt
Entry: A0A0Q9LVN2_9BACL
LinkDB: A0A0Q9LVN2_9BACL
Original site: A0A0Q9LVN2_9BACL 
ID   A0A0Q9LVN2_9BACL        Unreviewed;       370 AA.
AC   A0A0Q9LVN2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=NlpC/P60 domain-containing protein {ECO:0000259|PROSITE:PS51935};
GN   ORFNames=ASL11_31995 {ECO:0000313|EMBL:KRE57532.1};
OS   Paenibacillus sp. Soil750.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE57532.1, ECO:0000313|Proteomes:UP000051252};
RN   [1] {ECO:0000313|EMBL:KRE57532.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE57532.1,
RC   ECO:0000313|Proteomes:UP000051252};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE57532.1, ECO:0000313|Proteomes:UP000051252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil750 {ECO:0000313|EMBL:KRE57532.1,
RC   ECO:0000313|Proteomes:UP000051252};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRE57532.1}.
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DR   EMBL; LMSD01000042; KRE57532.1; -; Genomic_DNA.
DR   RefSeq; WP_056624183.1; NZ_LMSD01000042.1.
DR   AlphaFoldDB; A0A0Q9LVN2; -.
DR   STRING; 1736398.ASL11_31995; -.
DR   Proteomes; UP000051252; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..370
FT                   /note="NlpC/P60 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038577222"
FT   DOMAIN          238..369
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000259|PROSITE:PS51935"
FT   REGION          25..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  40418 MW;  5C32A582B2DB3467 CRC64;
     MWNKLKIPAI GSVIVVLAIS TACGKDNASP RSVTPSQSPT GMTGPGNSVP KSMSQAGKEI
     IALANNDAVL PMKQIGNVNY VSAQDLIRTL KFQSEWEDSE GKLILGDNDA NFELIMNSNK
     AMKDGADIQL SQPVVKEGGT AYLPVSDLAD LFQDDMSYEV RKGDVIVHAS PVAIIEHEDD
     PAGANDNSPE LNFGDDPTDP FKGNGAGANP AGMPIQTQHD LQVWSPNDQN DVMPVLKNID
     INALINKGEN YMGVKYKFGT GPYPQTGRFD CSTFTQYIFG KYNIKLPRVA RQQGTKGNLV
     SRKSLRKGDL MFFYVPGRFK SNKTVGHVGI YIGNMKMLHA SPEPKNGVQI SNIDKAYWKK
     TFLKAKRIAY
//
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