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Database: UniProt
Entry: A0A0F2C1E9_9MICO
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ID   A0A0F2C1E9_9MICO        Unreviewed;       327 AA.
AC   A0A0F2C1E9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KJQ52667.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:KJQ52667.1};
GN   ORFNames=RS85_03560 {ECO:0000313|EMBL:KJQ52667.1};
OS   Microbacterium sp. SA39.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ52667.1, ECO:0000313|Proteomes:UP000033425};
RN   [1] {ECO:0000313|EMBL:KJQ52667.1, ECO:0000313|Proteomes:UP000033425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA39 {ECO:0000313|EMBL:KJQ52667.1,
RC   ECO:0000313|Proteomes:UP000033425};
RA   Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJQ52667.1}.
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DR   EMBL; JXRU01000039; KJQ52667.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2C1E9; -.
DR   STRING; 1263625.RS85_03560; -.
DR   PATRIC; fig|1263625.4.peg.3579; -.
DR   Proteomes; UP000033425; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   PANTHER; PTHR46825:SF7; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:KJQ52667.1};
KW   Hydrolase {ECO:0000313|EMBL:KJQ52667.1};
KW   Protease {ECO:0000313|EMBL:KJQ52667.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT   DOMAIN          1..314
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   327 AA;  34494 MW;  89681A227C05CDE2 CRC64;
     MAGYDVPGAA VGVWIPGEGS WTSATGIADV EAGAPVDSDM AWPLRSVTKS YTVTLLLQLV
     DEGEASLDDT IGQYVDGVTA GDEITLRQLA EMSSGNADYT DDDFIAAFIE DPETVFTLDE
     LNGFMLGKPA QFAPGSEKVY TNANTNLLGA VIEKVTGQDF ADVLDERILA PLGQTGTRYI
     VDAATWREPH AVGYAPDEGT LAPQPENQSI FGPAGSMVST LDDALVWGQT LGTGVLLEPA
     TQKERQEGAP LDAGPPYDIY ALGIGETDGW WGHNGEGLGF TAAVFHHPES GATVAAFMNA
     SNLADRAHPA DQMFRAVARI LAAEADR
//
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