ID   A0A1C6V0L2_9ACTN        Unreviewed;       527 AA.
AC   A0A1C6V0L2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SCL59560.1};
GN   ORFNames=GA0070603_2839 {ECO:0000313|EMBL:SCL59560.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL59560.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL59560.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL59560.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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; FMIB01000002; SCL59560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6V0L2; -.
DR   STRING; 47854.GA0070603_2839; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000198605; 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:SCL59560.1};
KW   Hydrolase {ECO:0000313|EMBL:SCL59560.1};
KW   Protease {ECO:0000313|EMBL:SCL59560.1}; 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_5038640035"
SQ   SEQUENCE   527 AA;  55603 MW;  3200D55C8A5D7BB3 CRC64;
     MHRRLFPRAL AVLALVATAA TAGAPTATAE APTPAQTRLH ATIDAILADS RLAGAQAGVV
     VVDTTTGQTL YDRNGERRLV PASNTKLLTS TAAMELLGPG HRFTTDVSGD GVRHAGLLSG
     NLYLRGGGDP TMLAEDYDRL AAEVAAAGVR VVTGNLVADD TRYDRTRLGP DWTWDDESYY
     YAAQVSALTV APNTDYDAGT VIVHAAPAGQ AGTRPKITMT PANGWLRIDN RAETVATGET
     TISFEREHGG NTIVVTGQIA VGQAEESDWM TVWEPTGYAA DIFRSALQRH GVRVLGRTVL
     GQATPDDAKP VARHDSMPLA DLMVPFLKLS NNGHAEVLTK ELGRVLSGSG TWGAGLTAIS
     EYVGDSGMDT GTLRQRDGSG LSRRNMIPPA QFVALLTAVR AEPWFDTWYA ALPVAGNPER
     FVGGTLRSRM RGTAAADNVH AKTGSLTGAS SLSGYATDAD GHVLAFSIVL NNYLTSSVKG
     LEDQIAIALA SYTEKGTTTA RLAVPTAPES PRVPEGLECS WVKPIVC
//