ID   A0A1A9C431_9ACTN        Unreviewed;       481 AA.
AC   A0A1A9C431;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SBT95227.1};
GN   ORFNames=GA0115233_11243 {ECO:0000313|EMBL:SBT95227.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT95227.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; FLSP01000124; SBT95227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9C431; -.
DR   STRING; 1839783.GA0115233_11243; -.
DR   Proteomes; UP000198690; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SBT95227.1};
KW   Hydrolase {ECO:0000313|EMBL:SBT95227.1};
KW   Protease {ECO:0000313|EMBL:SBT95227.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198690}.
FT   REGION          33..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  48909 MW;  EF2E782A27A1803C CRC64;
     MSSQVTRPKT WQYTAGAATA GLALAVGVVT AAGPWDSSGQ RTAERDRAAA ERPTGGADHG
     RNSATTDRAP RPAPSAATVL TGLGGATGGA KPAPRTKALA KLLDPLLDAP ALGDRQSAAV
     VDITTGKRLY GDGAGTALTP ASTTKIATAA AVLSALGPDH RLTTRAALEP DTGELVLVGG
     GDPTLTARED AKGFASLRAL AEDTAAALKK DGVREVTLSY DTTLYAGDEL HPIGVDDNIA
     RITALMADEA RADDSTSGHA PRVPEPAVEA ARTFADLLKD HGIKTTPPGP SKATNRARTL
     AEVTSPPLSV LVERMLTNSD NDIAEALARH TALATGERPD LEGAGKAIKA ELGKLGLPMK
     GTEFQDGSGL DRDNLLTADL LTSLLTKSAD PAHPELRPIL TGLPVAGFTG TLTTRYESGA
     AGLVRAKTGT LTGVNALAGT VVDEDGHLLA FAFLATGTPN TPEARSALDE AATALAACGC
     T
//