ID   R1H209_9GAMM            Unreviewed;       478 AA.
AC   R1H209;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EOD54681.1};
GN   ORFNames=G113_13049 {ECO:0000313|EMBL:EOD54681.1};
OS   Aeromonas molluscorum 848.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD54681.1, ECO:0000313|Proteomes:UP000013526};
RN   [1] {ECO:0000313|EMBL:EOD54681.1, ECO:0000313|Proteomes:UP000013526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=848 {ECO:0000313|EMBL:EOD54681.1,
RC   ECO:0000313|Proteomes:UP000013526};
RX   PubMed=23788549;
RA   Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA   Bosch E.;
RT   "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT   Bivalve Molluscs.";
RL   Genome Announc. 1:E00382-13(2013).
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:EOD54681.1}.
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DR   EMBL; AQGQ01000089; EOD54681.1; -; Genomic_DNA.
DR   RefSeq; WP_005902987.1; NZ_AQGQ01000089.1.
DR   AlphaFoldDB; R1H209; -.
DR   MEROPS; S13.001; -.
DR   PATRIC; fig|1268236.3.peg.2566; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000013526; 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   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:EOD54681.1};
KW   Hydrolase {ECO:0000313|EMBL:EOD54681.1};
KW   Protease {ECO:0000313|EMBL:EOD54681.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..478
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004349872"
SQ   SEQUENCE   478 AA;  51871 MW;  EF52D759E0216123 CRC64;
     MQRFLIGFCA FVSLAAQAAT LTPPQGGQYA VIVQGNNGVE YARHADDMIA PASTMKVLTA
     LAARLELGAD FRFATEIQVK PGSKQGDLIN GDLWINFVGD PTLSRMDLLA LFKQLGVTRI
     KGNVHVNTGA YNGYERGNGW SWGDQTLCFA APVSAVIIDK NCAYGTVSAT QIGGPATGHV
     ATGVPISISA DNVDVMTYGD MARQFCALEV DMAKGNHYEL KGCITPNKEP QGLRFAIHDV
     EAWGWDNIRW AMDRAGVKHD GLLRVTHKAP EGAETLATHY SAPLPVMLAK MLKKSDNTYA
     DTFLKTVGRH YYNKPGSYRS GTMAVRAILT KQGIDLGNAT LADGSGLSAH NLISARQMLS
     VLNFIQRNDA QLGFIKLLPS SQVDGTLAWR RSVTAPMMKN KVHAKTGTIT GTSNLAGFID
     TAGGQRKAFV VFQRGLSQDP ATHERYRASK APWPWTVFEK GILEGIYQQQ PLQIVDRP
//