ID   A0A0M8XMI8_9ACTN        Unreviewed;       527 AA.
AC   A0A0M8XMI8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KOX09169.1};
GN   ORFNames=ADK66_13100 {ECO:0000313|EMBL:KOX09169.1};
OS   Micromonospora sp. NRRL B-16802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX09169.1, ECO:0000313|Proteomes:UP000037709};
RN   [1] {ECO:0000313|EMBL:KOX09169.1, ECO:0000313|Proteomes:UP000037709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX09169.1,
RC   ECO:0000313|Proteomes:UP000037709};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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:KOX09169.1}.
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DR   EMBL; LGEB01000054; KOX09169.1; -; Genomic_DNA.
DR   RefSeq; WP_053655116.1; NZ_LGEB01000054.1.
DR   AlphaFoldDB; A0A0M8XMI8; -.
DR   STRING; 1415541.ADK66_13100; -.
DR   PATRIC; fig|1415541.3.peg.2743; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000037709; 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; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KOX09169.1};
KW   Hydrolase {ECO:0000313|EMBL:KOX09169.1};
KW   Protease {ECO:0000313|EMBL:KOX09169.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..527
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038588553"
FT   REGION          496..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  55395 MW;  53255BABE5D3C2E1 CRC64;
     MHRRLFPRAL ALLALVATAA TAGAPGATAE SPTPATTRLR ATIDAILADN RLAGAQASVV
     VVDTSTGQTL YDRNGDRRLI PASNTKLLTS TAAMELLGPG HRFTTDVQTT GKRRGGLLSG
     NLHLRGGGDP TMLAADYDAL AAQVAADGVR VVSGNLIADD TRYDNTRLGP DWTWDDEPYY
     YAGQVSALTV APDTDYDAGT VIVHAAPAAR AGARPVVSTT PPTRYVRIDN RAETVSEGET
     SISIEREHGG NTIVVTGQIA VGDEPASDWV TVWEPTGYAA EVFRAALHRH GVRVLGRTVL
     GQPTPETAHL VARHDSMSLG ELMTPFLKLS NNGHAEVLTK EIGRVLSGSG TWSAGLTAIS
     EYVADTGMDT GTLRQRDGSG LSRRNLVPAA EFVDLLAEVR AEPWFATWYA ALPIAGQPDR
     FVGGTLRSRM AGTPAAGNVH AKTGSLTGVS GLSGYVTTAD GHLLAFSILL NNYLTASVKT
     LEDQIAVALA GHREGGTSTA RVAPPSVPDT PRTPEGVECS WVKPITC
//