ID K6DPG2_9BACI Unreviewed; 396 AA.
AC K6DPG2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Gamma-D-glutamyl-L-diamino acid endopeptidase 1 {ECO:0000313|EMBL:EKN70058.1};
GN ORFNames=BABA_06766 {ECO:0000313|EMBL:EKN70058.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70058.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN70058.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:EKN70058.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJLS01000043; EKN70058.1; -; Genomic_DNA.
DR RefSeq; WP_007084378.1; NZ_AJLS01000043.1.
DR AlphaFoldDB; K6DPG2; -.
DR STRING; 1117379.BABA_06766; -.
DR MEROPS; M14.008; -.
DR PATRIC; fig|1117379.3.peg.1418; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG2866; Bacteria.
DR OrthoDB; 9802862at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00118; LysM; 2.
DR CDD; cd06229; M14_Endopeptidase_I; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034274; ENP1_M14_CPD.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00257; LysM; 2.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT DOMAIN 1..45
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 51..95
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 264..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45272 MW; 588A6F338071FFC6 CRC64;
MDIFVRKGDS LWHYSQLFKI NLQLINDSNR DIQPNSLSIG QRIRIPGFVA QEQQIRQGDT
MWKLAQNRNL SIEALLLVNP TIDPNQLKIG QTIKIPLRIT WRLVNGGQNY DYKMMMNDIK
RLQGVYPFLQ VPTIGNTVLG KTIPEILIGN GRKKVHYNGS FHANEWITTP VIMTFLNDYL
LSLTNQNPIR GLTTSPFYQQ STLSIVPMVN PDGVDLVLHG SPANEPWKKK VVEYNKGSMD
FSGWKANIRG VDLNDQFPAR WELEKARNPD KPGPRDYGGE KPLSEPEAVA MAELTKKRDF
LRVLAFHTQG EVIYWGFENA EPPESEVIVK EFSRVSGYEP VKTIESYAGY KDWFIQDWHR
PGFTVEIGRG VNPLPISQFD EIYQKTLGIF LAGLYM
//
