ID   A0A090IK09_9GAMM        Unreviewed;       468 AA.
AC   A0A090IK09;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CED70562.1};
DE            EC=3.4.-.- {ECO:0000313|EMBL:CED70562.1};
GN   Name=dacB {ECO:0000313|EMBL:CED70562.1};
GN   ORFNames=AWOD_I_0468 {ECO:0000313|EMBL:CED70562.1};
OS   Aliivibrio wodanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=80852 {ECO:0000313|EMBL:CED70562.1, ECO:0000313|Proteomes:UP000032427};
RN   [1] {ECO:0000313|Proteomes:UP000032427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA   Hjerde E.;
RL   Submitted (SEP-2014) 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; LN554846; CED70562.1; -; Genomic_DNA.
DR   RefSeq; WP_045101261.1; NZ_LN554846.1.
DR   AlphaFoldDB; A0A090IK09; -.
DR   STRING; 80852.AWOD_I_0468; -.
DR   MEROPS; S13.001; -.
DR   GeneID; 28540014; -.
DR   KEGG; awd:AWOD_I_0468; -.
DR   PATRIC; fig|80852.17.peg.475; -.
DR   HOGENOM; CLU_017692_1_1_6; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000032427; Chromosome 1 complete 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:CED70562.1};
KW   Hydrolase {ECO:0000313|EMBL:CED70562.1};
KW   Protease {ECO:0000313|EMBL:CED70562.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..468
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001857501"
SQ   SEQUENCE   468 AA;  51758 MW;  2CA1DE28FE8F77AE CRC64;
     MSFSRFTLLG LALLSCSSFA SIQHALNTLP AGSRTAIVVE NLTSQDIEFQ QKQDELLPPA
     STLKIATALA ARLALGKEFT FSTNLNKIDN DVVLTFSGDP SLSRNDLSLI FDESDLKTIQ
     GDLWINDTIF TGYERAVGWP WDILGVCYSA PSSALSIDGN CVQASITTHT DGTTKVFVPI
     HQPILFSSTA LSVTREEQKV SFCDLELTTQ GNYYQLDGCL VERSKPLPLK FAIQDTQDFT
     KKTVLKILTE NNISLKGKVR FGNPVMPLES SLLLAQHKSK PLMELISHML KKSDNHYADN
     LIKMMGHLTY QQAGSFANGT AAMKDILLNQ ANIDLSNAVL VDGSGLSRNN RMTANQMKSI
     LQFIYKYDNE LDLIALLPIS GIDGTLKYRN SMRTEPIKGN ITAKSGSLFG SYNMAGFVGL
     KTNKAHLFVQ FVADYHPKKV KEASIPVERP IDTFEKEFYL EIIKLSTK
//