ID   E3EHG8_PAEPS            Unreviewed;       419 AA.
AC   E3EHG8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:ADO56121.1};
GN   Name=mlpA {ECO:0000313|EMBL:ADO56121.1};
GN   ORFNames=PPSC2_10140 {ECO:0000313|EMBL:ADO56121.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56121.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO56121.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO56121.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP002213; ADO56121.1; -; Genomic_DNA.
DR   RefSeq; WP_013370730.1; NC_014622.2.
DR   AlphaFoldDB; E3EHG8; -.
DR   STRING; 1406.LK13_22610; -.
DR   MEROPS; M16.A15; -.
DR   KEGG; ppm:PPSC2_10140; -.
DR   PATRIC; fig|886882.15.peg.2137; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_3_3_9; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000006868; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ADO56121.1};
KW   Protease {ECO:0000313|EMBL:ADO56121.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   DOMAIN          11..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..337
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   419 AA;  47121 MW;  005FE61A3BD6D398 CRC64;
     MERIQLKNGL RVVIEKIPTV RSVSFGIWVK TGSRNETSDN SGISHFIEHM LFKGTERFSA
     KEIAEQFDAI GGNVNAFTSK EYTCYYAKVL DEHLPIAVDV LSDMFFNSKL DQEELAREKN
     VILEEISMYE DTPDDMVHDL VSRAAYGEHP LAYPILGTED HLLAMDSSHL SHYMKEHYTI
     DNTVISVAGN VDDRLLELLE QHFGHFDNHG TVSPLTVPAF NGQLLYHEKA TEQNHICLSL
     PGFAIGDDLQ YAMVLLNNAI GGGMSSRLFQ EIREKRGLAY SVYSYHSSHA DSGMFTIYAG
     TAPKQTKDVL DLTLELLRDV AVNGLDANEL RKGKEQLKGS LILSLESTGS RMNRLGKNEL
     MLGQHYTLDQ MIEHIEQVTA DDVNKVLDRM FSEPFALSMV GASDSAVKDM RRDYFVNLR
//