ID A0A1X6YUE5_9RHOB Unreviewed; 494 AA.
AC A0A1X6YUE5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:SLN31502.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:SLN31502.1};
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:PSK87583.1};
GN Name=dacB {ECO:0000313|EMBL:SLN31502.1};
GN ORFNames=CLV79_10263 {ECO:0000313|EMBL:PSK87583.1}, LOS8367_01147
GN {ECO:0000313|EMBL:SLN31502.1};
OS Limimaricola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN31502.1, ECO:0000313|Proteomes:UP000193495};
RN [1] {ECO:0000313|EMBL:SLN31502.1, ECO:0000313|Proteomes:UP000193495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN31502.1,
RC ECO:0000313|Proteomes:UP000193495};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSK87583.1, ECO:0000313|Proteomes:UP000240624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK87583.1,
RC ECO:0000313|Proteomes:UP000240624};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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; PYGB01000002; PSK87583.1; -; Genomic_DNA.
DR EMBL; FWFY01000003; SLN31502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YUE5; -.
DR OrthoDB; 5372081at2; -.
DR Proteomes; UP000193495; Unassembled WGS sequence.
DR Proteomes; UP000240624; 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; 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:SLN31502.1};
KW Hydrolase {ECO:0000313|EMBL:SLN31502.1};
KW Protease {ECO:0000313|EMBL:SLN31502.1}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 52681 MW; F4D5B0E82D7ECC98 CRC64;
MAASATMAQP LTSLRPQARP DGAVALDAQP SGLRPKLRDS TARFVEEARL GGRTGFVALD
ARTGEILDQH DAYTRLPPAS VAKAITALYA LEALGGDFRF ETTLVATGPI ENGIVQGDLV
LAGTGDPTLD TDALAEMALK LKAMGVRGVA GGLAVWGGAV PQQSQIDPVQ LPHLGYNPAV
SGLNLNYNRI YFSWARSGGD YELSLDARGT NTRPEVSLAT MEAVDRGTPV YTYAQEDGVD
VWTVGRRYLG DSGSRWLPVR RPALYAGQVF AALAEEQGIE LGTVSEAASA PRGTVLVRHQ
SADLTKLIRD MLLYSTNLIA EQIGLAASVA RGTGVTDLPG SGRAMSDWVE ARFGAAPDLV
DHSGLGGASR ISAMQMAKIL ATPQAREELR PLLKSIRLFG PRGEALPRPP GVVVAKTGTL
NFVSALAGYE RTLGGRDIAF AIFSGDVARR IDAQDEEEER PEGARTYNSR AKWLQQRLLQ
RWGIAYSAKA ETTN
//
