ID F1VYP7_9BURK Unreviewed; 403 AA. AC F1VYP7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 03-MAY-2023, entry version 38. 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=IMCC9480_2662 {ECO:0000313|EMBL:EGF32266.1}; OS Oxalobacteraceae bacterium IMCC9480. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae. OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF32266.1, ECO:0000313|Proteomes:UP000004494}; RN [1] {ECO:0000313|EMBL:EGF32266.1, ECO:0000313|Proteomes:UP000004494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF32266.1, RC ECO:0000313|Proteomes:UP000004494}; RX PubMed=21572000; DOI=10.1128/JB.05088-11; RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.; RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing RT betaproteobacterium isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3421-3421(2011). CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}. 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:EGF32266.1}. 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; AEPR01000258; EGF32266.1; -; Genomic_DNA. DR AlphaFoldDB; F1VYP7; -. DR EnsemblBacteria; EGF32266; EGF32266; IMCC9480_2662. DR UniPathway; UPA00219; -. DR Proteomes; UP000004494; 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; IPR015956; Peniciliin-bd_prot_C_sf. 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 SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, KW ECO:0000313|EMBL:EGF32266.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000004494}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 297..387 FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C- FT terminal" FT /evidence="ECO:0000259|SMART:SM00936" FT ACT_SITE 79 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 82 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 141 FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2" SQ SEQUENCE 403 AA; 43928 MW; 33B7AEB29D97D10A CRC64; MFHHAMALPA RRLPLTLMKI FIAALAATVI SLSSVFVQPA SAQTMPAPIV AAKSWLLLDT TSGQVLASQD PTMRIEPASL TKIMTAYVTF QAIKEKRLDL AQMVNVSVRA WKVDPSSSKM FIDPATPVSV DDLLHGLMVQ SGNDAAVALA EAVAGTEEAF VVLMNREAKR MGLTNTQFGN PHGLPSQSNY STAQDLSKLA AAVITDYPEF YKIDSVKSFT YNKITQPNRN RLLWLDPSVD GMKTGHTEAA GYCIIASAKR PNGSGERRLI SVVLGANSDQ SRTQESQKLL NWGFQNFDTV KLYGKGQPVE TPPVWKGSEK TIKIGFTQDI YVTVAKGVAA KMKPVLERKD PLVAPIAANS KVGMMKMMVD GKSIAEFPIL ALENVNEAGI FGRAWDSIRL WIQ //