ID   A0A1C5ITU0_9ACTN        Unreviewed;       527 AA.
AC   A0A1C5ITU0;
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:SCG61421.1};
GN   ORFNames=GA0070213_10762 {ECO:0000313|EMBL:SCG61421.1};
OS   Micromonospora humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG61421.1, ECO:0000313|Proteomes:UP000199360};
RN   [1] {ECO:0000313|EMBL:SCG61421.1, ECO:0000313|Proteomes:UP000199360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG61421.1,
RC   ECO:0000313|Proteomes:UP000199360};
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; FMDM01000007; SCG61421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5ITU0; -.
DR   STRING; 745366.GA0070213_10762; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000199360; 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:SCG61421.1};
KW   Hydrolase {ECO:0000313|EMBL:SCG61421.1};
KW   Protease {ECO:0000313|EMBL:SCG61421.1}; 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_5038727995"
SQ   SEQUENCE   527 AA;  55617 MW;  467B756F3B4196EF CRC64;
     MHRRLFPRAL AALVLVATAA TAGAPTATAE APTPAQTRLH ATIDAVLADS RLDGAQAGVV
     VVDTATGRTL YDRNGNRRLV PASNTKLLTS TAAMELLGPG HRFTTDVSAG GPRRAGLLSG
     DLYLRGGGDP TMLAADYDRL AGQVAATGVR VVTGDLVADD TRYDRSRLGP DWTWDDEPYY
     YAAQVSALTV APDTDYDAGT VIVNATPGAR AGARPRISMT PDNGWLRIDN RAETVADGET
     TISIEREHGG NTVVVTGQIA VGQATESDWV TVWEPTGYAA DVFRSALRRH GVRVLGRTVL
     GTATPDSARP LARHDSMPLS DLMVPFLKLS NNGHAEVLTK ELGRVLSGSG SWAAGLTAIG
     EYVGDAGMDT GTLRQRDGSG LSRRNLIPPA QFVTLLSAVR GEPWFDTWYA ALPVAGNADR
     FVGGTLRSRM AGTAAANNVH AKTGSLTGVS GLSGYVTDAD GRLLAFSIVL NNYLTSSVKG
     LEDQIAIALA SYTERETATA RRTVPTAPDS PRVPEGRECS WVKPVRC
//