ID   A0A0F4RMC9_9RHOB        Unreviewed;       488 AA.
AC   A0A0F4RMC9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KJZ20784.1};
GN   ORFNames=TW80_08530 {ECO:0000313|EMBL:KJZ20784.1};
OS   Loktanella sp. S4079.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20784.1, ECO:0000313|Proteomes:UP000033741};
RN   [1] {ECO:0000313|EMBL:KJZ20784.1, ECO:0000313|Proteomes:UP000033741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4079 {ECO:0000313|EMBL:KJZ20784.1,
RC   ECO:0000313|Proteomes:UP000033741};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ20784.1}.
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DR   EMBL; JXYE01000002; KJZ20784.1; -; Genomic_DNA.
DR   RefSeq; WP_045996800.1; NZ_JXYE01000002.1.
DR   AlphaFoldDB; A0A0F4RMC9; -.
DR   STRING; 579483.TW80_08530; -.
DR   PATRIC; fig|579483.3.peg.1750; -.
DR   Proteomes; UP000033741; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KJZ20784.1};
KW   Hydrolase {ECO:0000313|EMBL:KJZ20784.1};
KW   Protease {ECO:0000313|EMBL:KJZ20784.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033741}.
SQ   SEQUENCE   488 AA;  53060 MW;  8E23AA3A468DB74B CRC64;
     MKLTRRGLLG GAASVMATGA LAEAPMRSLR PVLRPSYPDR IARLIARAGV TGDVSVILTD
     AHTKEIVEEH RSDTLLPPAS VTKAVTALYA IENLGADHQF QTIVYADGEI VDGVLDGNLI
     LAGGGDPNLV TDDLAELAQR LKNTGLREVR GAFFVWDEAL VNLDEIDSTQ LDYLGYNPTV
     TGLNLNFNRV HFEWKLEGGN YTTAMDARSE NYRPAVTSSR IRIEDRNTPV FTYRDLGEVD
     QWTVARRALN NGGSRWLPVR HPALYAGEVF ATFARAQGIV LSPPKEIAAL PATRVALAHF
     AGKPLTDVMR AMMRYSTNIT AEAAGLAATK IDTGQKWGLR ASAARMSRWA RDRGQGIRAD
     FADHSGLGDQ SRVGASDMVQ FLTAPNVLQT LRPIMKDIPV VDSADNRVAS AAGAVQAKTG
     TLNFVSNLAG YLRGSDGRDL AFAIFVADMD ARERGKLEGG EAPRGSRQWN RRAKSLQESL
     IYQWTTAL
//