ID A0A149VRZ8_9PROT Unreviewed; 477 AA.
AC A0A149VRZ8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:KXW56000.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KXW56000.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KXW56000.1};
GN Name=dacB {ECO:0000313|EMBL:KXW56000.1};
GN ORFNames=FV185_11610 {ECO:0000313|EMBL:KXW56000.1};
OS Ferrovum sp. PN-J185.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=1356306 {ECO:0000313|EMBL:KXW56000.1, ECO:0000313|Proteomes:UP000075387};
RN [1] {ECO:0000313|EMBL:KXW56000.1, ECO:0000313|Proteomes:UP000075387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN-J185 {ECO:0000313|EMBL:KXW56000.1,
RC ECO:0000313|Proteomes:UP000075387};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain PN-
RT J185.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXW56000.1}.
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DR EMBL; LQZA01000002; KXW56000.1; -; Genomic_DNA.
DR RefSeq; WP_067494872.1; NZ_LQZA01000002.1.
DR AlphaFoldDB; A0A149VRZ8; -.
DR STRING; 1356306.FV185_11610; -.
DR PATRIC; fig|1356306.3.peg.1153; -.
DR InParanoid; A0A149VRZ8; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000075387; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KXW56000.1};
KW Hydrolase {ECO:0000313|EMBL:KXW56000.1};
KW Protease {ECO:0000313|EMBL:KXW56000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075387}.
SQ SEQUENCE 477 AA; 53822 MW; 6D4C7444A54DF50C CRC64;
MQISRVLVSK ICYLFITVCL FTLNKVNAEG LPQPLATLLK DLNIPEEHVG LIVQKVGAPT
PLLSLNKDKQ YQPASVIKIV TAYSSLSLLG PNYAWLTSIH GELDKHSQLV GDLVVQAQGD
PLLTLENWSQ LWRELYLLGV HEIHGNIIID NARYQINYQD PNLFDHQGDR VYNLVPHPLT
IDFDRFALNI TPINHSIYVN SNFNWPDTVI VNEVKPVDLP CPHDVEESIQ VFAQQQGDQT
HIHVTGEWPI SCGIGQLSRR LLPNERVISS SIVQIWQQLG GKFDGKIIFN QSYKKLPELV
SNHSLPLFVL IPLMDKYSNN VIARMIYLSV GNPDATQKTS FEQAEKNIRD FLQRKGIDTK
PLVIKNGSGL SRESSLSPQF LNSLLQVIWQ DPLGHEVIAS LPLMGSEGTL IRKQTNSFEI
NKMYLKTGTL KSVKAVAGYV QTKKGQWYTV TCLINDDNAA TSMPFIHRLL DWIYLTR
//
