ID A0A2N6N9P2_BEABA Unreviewed; 542 AA.
AC A0A2N6N9P2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:PMB63987.1};
GN Name=DAC_1 {ECO:0000313|EMBL:PMB63987.1};
GN ORFNames=BM221_010150 {ECO:0000313|EMBL:PMB63987.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB63987.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB63987.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB63987.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- SIMILARITY: Belongs to the peptidase S12 family.
CC {ECO:0000256|ARBA:ARBA00038215}.
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:PMB63987.1}.
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DR EMBL; MRVG01000015; PMB63987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6N9P2; -.
DR OMA; KETHAPQ; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:PMB63987.1};
KW Hydrolase {ECO:0000313|EMBL:PMB63987.1};
KW Protease {ECO:0000313|EMBL:PMB63987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT DOMAIN 21..364
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59762 MW; 7D8BCF44465577D9 CRC64;
MPSQRNETVQ RGNPLSDEFG RYVKGLMDEW NVPGLSLAVI DGDQVYAEGY GFSVLPDTPV
KPETLFLGGS TTKAQVGAAL AHLISTGDYD TAFSRGWETP ISSIIEEDFV LKDEWATAHI
TLEDAISHRS GMPGHDFAWT GTSDPSDSNN TRKTNNTSKT NRATVRSLRH LPLTAEPRVV
FQYCNLMYIA LSHVIETVTG SWLGDVLRNV IWQPLGMNST FLSYSEARRS GHQIATGYFW
DDESQEYVAV ETDPVQYSSG AGAIITNAMD YSKWVKCLSH ETAPFSAATH QDIKTPRTLE
ITGGASRSWH VGDYGLGWRI ATLHGKAVYK HNGGTQNFGT NVFWMPEIKF GVVGFANAVD
NGNFIKDIIT QKLAEDRLGI SPSERLDDGQ KERKRQLEQD KQNFNNATNI LYPSYATNGA
SLAVDYDLFV GTYSSPGYGN YTFAVEDALP FPGANSTNQA LQKQLVATRA DLIIPMRMIL
RHVAGDYWVA YLIPILGSAA KRSFYAAKFV VGGDGKPTAL EITWQGAVER LSEVTTRFDR
VG
//
