ID A0A0B5DKV4_9ACTN Unreviewed; 544 AA.
AC A0A0B5DKV4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AJE41800.1, ECO:0000313|EMBL:QEV40333.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:QEV40333.1};
GN Name=dacB {ECO:0000313|EMBL:QEV40333.1};
GN ORFNames=CP978_18865 {ECO:0000313|EMBL:QEV40333.1}, SNOD_18545
GN {ECO:0000313|EMBL:AJE41800.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE41800.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE41800.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE41800.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV40333.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV40333.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) 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; CP009313; AJE41800.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV40333.1; -; Genomic_DNA.
DR RefSeq; WP_043442588.1; NZ_JACHMR010000001.1.
DR AlphaFoldDB; A0A0B5DKV4; -.
DR STRING; 40318.SNOD_18545; -.
DR KEGG; snq:CP978_18865; -.
DR HOGENOM; CLU_017692_0_2_11; -.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; 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; 3.40.710.10; 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; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AJE41800.1};
KW Hydrolase {ECO:0000313|EMBL:QEV40333.1};
KW Protease {ECO:0000313|EMBL:AJE41800.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526}.
FT REGION 86..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 55698 MW; FB6A776EDB8DFDFC CRC64;
MVVPELRPWR AARPHLARVA RAVTPRLARV AQAVRPRAQR ITEVVRPHVA RVTRAVRPRE
GRYTTPQVAA VAATVGLALA AGAATAAGPW DSTGQRTAER DRAAAWSREG GADHGSRSGA
AAETPAPAPS AAPVLAGVTG RTVLTKSAPS APSVPTLASV LDRLLDDDSL GPRRTAAVVD
VATGERLYGK DQDRALTPAS TTKIATAVAA LSAVGPDHRF VTRAVLEPGT DKLLLVGGGD
PTLTARGKGG AWADLRALAD RTATALEKRR LPRVSLAYDA SLFTGEDLHP IGVNENIARV
TALMADEGRT DDSGSGPAAR SADPAAEAAR TFGALLRDRG IEVEAPDAAA KATPDAATLA
SVQSPPLSAV VERMLTDSDN DIAEALARHT ALATGRDASF EGGAAAVHDR LGKLGLPVAG
SAFHDGSGLD REDKLTANLL TALLATAGSP SHPELRAALT GLPVAGFTGT LSDRYENTAE
RPGIGLVRAK TGSLTGVNTL AGIVVDADGR LLAFAFLTDG SMDQTAARAA LDRAAAALAG
CGCR
//
