ID   A0A1I0KP59_9ACTN        Unreviewed;       351 AA.
AC   A0A1I0KP59;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SEU27357.1};
GN   ORFNames=SAMN05421811_10910 {ECO:0000313|EMBL:SEU27357.1};
OS   Nonomuraea wenchangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=568860 {ECO:0000313|EMBL:SEU27357.1, ECO:0000313|Proteomes:UP000199361};
RN   [1] {ECO:0000313|EMBL:SEU27357.1, ECO:0000313|Proteomes:UP000199361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SEU27357.1,
RC   ECO:0000313|Proteomes:UP000199361};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOHX01000009; SEU27357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0KP59; -.
DR   STRING; 568860.SAMN05421811_10910; -.
DR   OrthoDB; 5496837at2; -.
DR   Proteomes; UP000199361; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14814; Peptidase_M15; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:SEU27357.1};
KW   Hydrolase {ECO:0000313|EMBL:SEU27357.1};
KW   Protease {ECO:0000313|EMBL:SEU27357.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199361}.
FT   DOMAIN          237..344
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          20..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  38416 MW;  9A38BF33D9AF4B79 CRC64;
     MVASLLVSSA QVVVAEASAQ VERRGQERQD PGNLTELRKE AERSAKELEE ATKALEKRRS
     TIAASEKQLK GKLTALQELE RRLAVMRQPV SQMAELLYVQ PLNGGGVLPF LAGGADENTL
     RALSDANQIV ATRQQAVQQT SALYAQAEQL ASEAQELRAG NLLAEAQLAA EIDTLRQRSD
     KIVKSLTAAL VKLGIKIDKV GRAALGCDPL RAATAGEYPN GLIPRGMLCP LQQKGFSLRA
     DATIAFVSLN EAFKQRFGKQ MCVTDAYRSL AEQQAVYYRR PGFAAVPGRS NHGLGLAVDL
     CGGVERSGSA EFVWMERNSK KYGWFHPSWA YSSPFEPWHW EYDPQLGSLL D
//