ID   A0A1H9RGQ9_9RHOB        Unreviewed;       494 AA.
AC   A0A1H9RGQ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SER71159.1};
GN   ORFNames=SAMN04490244_102242 {ECO:0000313|EMBL:SER71159.1};
OS   Tranquillimonas rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=641238 {ECO:0000313|EMBL:SER71159.1, ECO:0000313|Proteomes:UP000198885};
RN   [1] {ECO:0000313|EMBL:SER71159.1, ECO:0000313|Proteomes:UP000198885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23042 {ECO:0000313|EMBL:SER71159.1,
RC   ECO:0000313|Proteomes:UP000198885};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOGU01000002; SER71159.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9RGQ9; -.
DR   STRING; 641238.SAMN04490244_102242; -.
DR   Proteomes; UP000198885; 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; 1.
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:SER71159.1};
KW   Hydrolase {ECO:0000313|EMBL:SER71159.1};
KW   Protease {ECO:0000313|EMBL:SER71159.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198885};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..494
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011446307"
SQ   SEQUENCE   494 AA;  53570 MW;  2C883B47927EB5D4 CRC64;
     MASSNDPMRL TRRALLGGLM AGVAGPALAD APERSRRPLP RPDGLYKQAQ AAADELVRRA
     GLTGEVGFAV ADVSTGLMLE TRSPLKGHPP ASTAKALTTL YARKTLGGDY RFGTELRTTG
     PLIDGKIDGD LILAGGGDPT LDTDALGALA ERLKEAGVRE ISGTFRVYTG ELPTVREIDI
     EQPDHVGYNP AVGGLNLNFN RVHFQWEKGS DGYNVSMDAR AARYRPDVTM ARMSVVERKS
     PVYTYEDSGG IDDWTVARWA LGGSGARWLP VRRPGEYAGE AFRVIARSHG IQLGREIGRS
     DRPGDFLLAR HESAPLDDIL RDMMKYSTNL TAEVVGLAAS TEIGGPVEDL HASAARMNAW
     LAEEYSARAT DLEDHSGLGD DSRVSPRDMV QALVQEGADS KLRDLMKEVS VPGRPDLKVK
     AKTGTLNFCS CLVGYLQAPG NTTLAFAIFT ADVERRDALP MEQRERPPGG RAWLARSRNL
     QKELLERWGV VFGT
//