ID A0A1J0AC55_9CYAN Unreviewed; 466 AA.
AC A0A1J0AC55;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:APB33506.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:APB33506.1};
GN Name=dacB {ECO:0000313|EMBL:APB33506.1};
GN ORFNames=GlitD10_1186 {ECO:0000313|EMBL:APB33506.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB33506.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB33506.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB33506.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017675; APB33506.1; -; Genomic_DNA.
DR RefSeq; WP_071454084.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0AC55; -.
DR STRING; 1188229.GlitD10_1186; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000180235; 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; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:APB33506.1};
KW Hydrolase {ECO:0000313|EMBL:APB33506.1};
KW Protease {ECO:0000313|EMBL:APB33506.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000180235}.
SQ SEQUENCE 466 AA; 51739 MW; 7F8AE0B8C83CEC00 CRC64;
MFLASPPAEV ELCRTSLTTA LDQVRQQPEY QKAHWGILIQ TQTAPPRTLY EHQSQQFFLP
ASTTKLLTTA GALVHLGGEH RLRTAFYQQG RQLHLVGQGD PTLTTVKLQQ LVQKITPAQR
QSFDTVVIQT GFFQGLNFND QWEWQDILNT DMVPVNNLIL NRNESQLRLI AQTAGKPARV
AWSDPYAVRY WQMINTTRST NNPIQPIQIW IPPGLPQLHI RGDVTSQPLS FTVPVLDTDQ
YLVQTLTRFF PHKKVEVRRT ILPANLGKEV AAVQSVPVTQ LVTQINQVSD NLYAEALLRH
LGAVSNPRIP SDLAGIQTVQ KVLGGLGVTP GGVLQKDGSG LSRHNRVTPA ALVQMLQGMA
ASSPYVNSLA APGLPGTLRR RFTQTDINLQ AKTGTLSGVA SLAGYLQPRN RPRLVFTIVV
NQSEQPATVL RRGIDQMVMT VNDWAERSTP DQWGNCTQTN ARQWVN
//
