ID   A0A0X8HEZ1_9GAMM        Unreviewed;       480 AA.
AC   A0A0X8HEZ1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase DacC {ECO:0000313|EMBL:AMD01410.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:AMD01410.1};
GN   Name=dacC_2 {ECO:0000313|EMBL:AMD01410.1};
GN   ORFNames=LOKO_02350 {ECO:0000313|EMBL:AMD01410.1};
OS   Halomonas chromatireducens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD01410.1, ECO:0000313|Proteomes:UP000063387};
RN   [1] {ECO:0000313|EMBL:AMD01410.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD01410.1,
RC   ECO:0000313|Proteomes:UP000063387};
RX   PubMed=26988058;
RA   Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA   Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA   Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT   "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT   Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|EMBL:AMD01410.1, ECO:0000313|Proteomes:UP000063387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD01410.1,
RC   ECO:0000313|Proteomes:UP000063387};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; CP014226; AMD01410.1; -; Genomic_DNA.
DR   RefSeq; WP_066449291.1; NZ_CP014226.1.
DR   AlphaFoldDB; A0A0X8HEZ1; -.
DR   STRING; 507626.LOKO_02350; -.
DR   KEGG; hco:LOKO_02350; -.
DR   PATRIC; fig|507626.3.peg.2343; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000063387; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:AMD01410.1};
KW   Hydrolase {ECO:0000313|EMBL:AMD01410.1};
KW   Protease {ECO:0000313|EMBL:AMD01410.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063387}.
SQ   SEQUENCE   480 AA;  51534 MW;  DB6F5C0AA352DC33 CRC64;
     MSRWLVLPLG LLLGLLLPLG AAGAGFPELE RMVERGFLVS AEAKLLDTGE VLGAIDPQRQ
     LSPASVTKAY LAAAALDRWG PQHRFTTRLA SDAELNGSGV VAGDLILEGG GDPALTTEDL
     WRLAQRLHQR GVREVEGRLV VSQWRFGPVE CITTDRCQAR TRTANAYSAL LSSAGVNYGS
     WCVSVAPGAA AGQPAQITSC DSQTTIVGID NQVETQPPNS GTELNAERVT RDDGDVMVLR
     GQISLNASPR EVYRASSDPA QQTARTMTAM LEQAGIAVRQ GYTTSVEEPP AAARTLAAVD
     GKPLQELLLR TMNYSNNFMA DVLALNLVDT PRSSLLQAGD AIEHYVAGMP DHGPLIMLSG
     SGLTTENRTS AHGSNILLES MFHRTALFPS FVASFQSPAN GVSRFIQRGS STFQNHVMLK
     TGTLNQPIAV RSVSGYFRTL SGRWGVFTVL VNGTATTPWL NWAQVLDPLA EDLERMIEAH
//