ID A0A0D6PN61_9PROT Unreviewed; 425 AA. AC A0A0D6PN61; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 08-NOV-2023, entry version 22. DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448}; DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448}; GN ORFNames=Gbfr_003_077 {ECO:0000313|EMBL:GAN89142.1}; OS Gluconobacter frateurii M-2. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1231354 {ECO:0000313|EMBL:GAN89142.1, ECO:0000313|Proteomes:UP000032669}; RN [1] {ECO:0000313|EMBL:GAN89142.1, ECO:0000313|Proteomes:UP000032669} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M-2 {ECO:0000313|EMBL:GAN89142.1, RC ECO:0000313|Proteomes:UP000032669}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Gluconobacter frateurii M-2."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also CC transpeptidation of peptidyl-alanyl moieties that are N-acyl CC substituents of D-alanine.; EC=3.4.16.4; CC Evidence={ECO:0000256|ARBA:ARBA00034000}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752}. CC -!- SIMILARITY: Belongs to the peptidase S11 family. CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}. 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:GAN89142.1}. 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; BANG01000003; GAN89142.1; -; Genomic_DNA. DR RefSeq; WP_048842533.1; NZ_BANG01000003.1. DR AlphaFoldDB; A0A0D6PN61; -. DR EnsemblBacteria; GAN89142; GAN89142; Gbfr_003_077. DR UniPathway; UPA00219; -. DR Proteomes; UP000032669; Unassembled WGS sequence. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR018044; Peptidase_S11. DR InterPro; IPR012907; Peptidase_S11_C. DR InterPro; IPR037167; Peptidase_S11_C_sf. DR InterPro; IPR001967; Peptidase_S11_N. DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1. DR PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1. DR Pfam; PF07943; PBP5_C; 1. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SMART; SM00936; PBP5_C; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000313|EMBL:GAN89142.1}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022670}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 318..408 FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C- FT terminal" FT /evidence="ECO:0000259|SMART:SM00936" FT ACT_SITE 107 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 110 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 167 FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2" SQ SEQUENCE 425 AA; 44670 MW; 9758A26996BF6E0A CRC64; MTAVTKAEKL GTNVRTRRSL FGGVAGFAAC ASFGGPLSAL ARPHHHAGHA KAAAAGASAA PAAPVGTPAN TPIGPFDTVA RWAYIVDFDT GAVLLDKAAD ERMAPSSLTK MMTAYIVFGM LATGRLRLDQ ALPVSEKAWR TQGSKMFVPL GESVAVQDLI QGMVIQSGND ACVVLAEGIA GSEERFVAMM NEEAPKIGLN NSHFMNVTGL PAEGHYMSAH DVATVAMHLI RDFPQYYHFF GETEFLFNKI KQGNRNVLVD KGLADGLKTG HTDAGGFGLC ASSNRNGNRV IVVINGTASS NERAHEGERL MAWAFANFEN ATLFRKGQVV DHAPVWMGER KAVPLVAGSD IVMTMPVGWQ QRSHIAVDYA SPVIAPVVAG QSCGAIVISA PGMADIRVAL QAGASVAKLG LVGRAMARLG HGPAN //