ID A0A073CFX6_PLAAG Unreviewed; 442 AA.
AC A0A073CFX6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Dac {ECO:0000313|EMBL:KEI67036.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KEI67036.1};
GN Name=dac {ECO:0000313|EMBL:KEI67036.1};
GN ORFNames=A19Y_2068 {ECO:0000313|EMBL:KEI67036.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI67036.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI67036.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI67036.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002803; KEI67036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073CFX6; -.
DR STRING; 388467.A19Y_2068; -.
DR MEROPS; S13.003; -.
DR PATRIC; fig|388467.6.peg.2017; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_047821_0_0_3; -.
DR Proteomes; UP000027395; 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 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:KEI67036.1};
KW Hydrolase {ECO:0000313|EMBL:KEI67036.1};
KW Protease {ECO:0000313|EMBL:KEI67036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395}.
SQ SEQUENCE 442 AA; 47513 MW; 23057386D2F257E7 CRC64;
MNMIDILSSG LVSVWLQMAG MDRAELNNSV LENLETELSQ VVFPQQPDPV AEAVVQQYLN
RLSAKGLSQD VQGVWVQSSW VPLAKNSGTT PLPAASLTKI ATSLASLQVW PPEHRFETIL
GVTGPIVGGV VQGDLVVTGN GDPFFIWEEA IALGNSLNQM GIRGVAGNLI ITDRFYMNYE
VDPMKVGQLL KEAFNSQSWK EEIIGQHSRM TPGTAKPQVV ISGNIIAQTG AVNSTPIIRH
QSLALVEIIK QMNIYSNNLM AEILAANVGG AANVRQLASQ AAGVPIDEIR LINGSGLEPE
NQISPRAVVG MFMALARYLQ DTNLTVADLF PIAGIDTQGT LEDRKIPVSS PVKTGTLSDV
SALAGVLPTR DRGLVWFAII NRGTNLDGLR ADQDLLLQQL VSKWGSPDSL PELIQPHIDG
RRPGIGDSTR NQILVQTVAP SS
//
