ID   V9GDT0_9BACL            Unreviewed;       294 AA.
AC   V9GDT0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:GAE07645.1};
GN   ORFNames=JCM10914_3885 {ECO:0000313|EMBL:GAE07645.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE07645.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE07645.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE07645.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
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:GAE07645.1}.
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DR   EMBL; BAUO01000015; GAE07645.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9GDT0; -.
DR   STRING; 1236974.GCA_001315105_03772; -.
DR   Proteomes; UP000018028; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14852; LD-carboxypeptidase; 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:GAE07645.1};
KW   Hydrolase {ECO:0000313|EMBL:GAE07645.1};
KW   Protease {ECO:0000313|EMBL:GAE07645.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018028};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..294
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038396829"
FT   DOMAIN          141..269
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          42..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  32106 MW;  262DCB84EFCE6E21 CRC64;
     MVEREKREMN GYTRTGFRLI SIALASLLLA GTVLAGCQSN DTGSGQGVGQ DLQSPADGQE
     GSTLPEGTPE DGVEADPVMA KRSENALQAT VQEQNGKQVV TNAEAMTVIV NKQRSLPDGY
     EPSDLVEPNV PFSFDEPHEK RHLRKEAADA LEKLFAAAKE DGIELRAVSG YRSYARQKTI
     YENNVRTKGE AEANRVSAVP GTSEHQTGLT IDVSSPSAGN ALEEVFGHTE EGQWLDRRGP
     EFGFIIRYPD GAEDITGYVY EPWHIRYIGT DLAPDIAESG LTLEEYFDEA NIKL
//