ID L3CEA0_ECOLX Unreviewed; 304 AA. AC L3CEA0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-APR-2021, entry version 25. DE SubName: Full=Murein tetrapeptide carboxypeptidase {ECO:0000313|EMBL:ELC98562.1}; GN ORFNames=A13W_00489 {ECO:0000313|EMBL:ELC98562.1}; OS Escherichia coli KTE193. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1181739 {ECO:0000313|EMBL:ELC98562.1, ECO:0000313|Proteomes:UP000010651}; RN [1] {ECO:0000313|EMBL:ELC98562.1, ECO:0000313|Proteomes:UP000010651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KTE193 {ECO:0000313|EMBL:ELC98562.1, RC ECO:0000313|Proteomes:UP000010651}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Escherichia coli KTE193."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the peptidase S66 family. CC {ECO:0000256|ARBA:ARBA00010233}. 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:ELC98562.1}. 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; ANTH01000009; ELC98562.1; -; Genomic_DNA. DR RefSeq; WP_001536892.1; NZ_KB732454.1. DR MEROPS; S66.002; -. DR EnsemblBacteria; ELC98562; ELC98562; A13W_00489. DR PATRIC; fig|1181739.3.peg.504; -. DR HOGENOM; CLU_034346_0_1_6; -. DR Proteomes; UP000010651; Unassembled WGS sequence. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10740; -; 1. DR Gene3D; 3.50.30.60; -; 1. DR InterPro; IPR027461; Carboxypeptidase_A_C_sf. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR027478; LdcA_N. DR InterPro; IPR040449; Peptidase_S66_N. DR InterPro; IPR040921; Peptidase_S66C. DR InterPro; IPR003507; S66_fam. DR PANTHER; PTHR30237; PTHR30237; 1. DR Pfam; PF02016; Peptidase_S66; 1. DR Pfam; PF17676; Peptidase_S66C; 1. DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1. DR SUPFAM; SSF141986; SSF141986; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 3: Inferred from homology; KW Carboxypeptidase {ECO:0000313|EMBL:ELC98562.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000313|EMBL:ELC98562.1}. FT DOMAIN 5..126 FT /note="Peptidase_S66" FT /evidence="ECO:0000259|Pfam:PF02016" FT DOMAIN 169..284 FT /note="Peptidase_S66C" FT /evidence="ECO:0000259|Pfam:PF17676" FT ACT_SITE 106 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1" FT ACT_SITE 200 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1" FT ACT_SITE 270 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1" SQ SEQUENCE 304 AA; 33725 MW; 82F6B1DDD3EA0E73 CRC64; MSLFHLIAPS GYCIKQHAAL RGIQRLTDAG HQVNNVEVIA RRCERFAGTE TERLEDLNSL ARLTTPNTIV LAVRGGYGAS RLLADIDWQA LVARQQYDPL LICGHSDFTA IQCGLLAQGN VITFSGPMLV ANFGADELNT FTEHHFWLAL RNETFTIEWQ GEGPICRAEG TLWGGNLAML ISLIGTPWMP KIENGILVLE DINEHPFRVE RMLLQLYHAR ILPRQKAIIL GSFSGSTPND YDAGYNLESV YAFLRSRLSI PLITGLDFGH EQRTVTLPLG AHAMLNNTHE GTQLTISGHP VLKM //