ID I0Q2F1_STROR Unreviewed; 413 AA. AC I0Q2F1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 12-AUG-2020, entry version 25. 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=HMPREF1115_0638 {ECO:0000313|EMBL:EIC75453.1}; OS Streptococcus oralis SK610. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1095741 {ECO:0000313|EMBL:EIC75453.1, ECO:0000313|Proteomes:UP000004548}; RN [1] {ECO:0000313|EMBL:EIC75453.1, ECO:0000313|Proteomes:UP000004548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK610 {ECO:0000313|EMBL:EIC75453.1, RC ECO:0000313|Proteomes:UP000004548}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. 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:ARBA00000871}; 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:EIC75453.1}. 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; AJKQ01000019; EIC75453.1; -; Genomic_DNA. DR RefSeq; WP_000720628.1; NZ_AJKQ01000019.1. DR MEROPS; S11.006; -. DR EnsemblBacteria; EIC75453; EIC75453; HMPREF1115_0638. DR PATRIC; fig|1095741.3.peg.1067; -. DR BioCyc; GCF_000257455-HMP:HMPREF1115_RS07595-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000004548; Unassembled WGS sequence. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro. DR Gene3D; 2.60.410.10; -; 1. DR Gene3D; 3.40.710.10; -; 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 Pfam; PF07943; PBP5_C; 1. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SMART; SM00936; PBP5_C; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR SUPFAM; SSF69189; SSF69189; 1. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..413 FT /note="Serine-type D-Ala-D-Ala carboxypeptidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003631914" FT DOMAIN 293..394 FT /note="PBP5_C" FT /evidence="ECO:0000259|SMART:SM00936" FT ACT_SITE 56 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 59 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT ACT_SITE 119 FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1" FT BINDING 239 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2" SQ SEQUENCE 413 AA; 45009 MW; A0363A12059303AB CRC64; MKKIILSFIT LLVFGTASTV SAQEFDVAAK HAIAVEATTG KILYEKDANQ PVEIASITKL VTVYLVYEAL EQGTIGLSTP VDISDYPYKL TTNSEASNVP MEARNYTVEQ LLEATMVSSA NSAAIALAEK IAGSEKDFVD KMRAKLLEWG IQDATIVNTT GLNNETLGDN IYPGSKKDDE NKLSAYDVAI VARNLIRDYP QVLEITKKPT STFAGLEIHS TNYMLEGMPA YRGGIDGLKT GTTDKAGASF VGTTVEKGMR IITVVLNADQ QDTNPYARFT ATSALLDYIS ANFALKTVVQ KGEAYNDSKV TVLDGKEDNV TAVAKSDISI VQRIGSGTTP ALQFTPKSTS EMAPLEEGKV VGTLTYDDQD LVGQGYLTSD KPSFEMVSEK KVEKAFFLKV WWNQFIRFIN EKL //