ID A0A6J4WI21_CORDP Unreviewed; 587 AA. AC A0A6J4WI21; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 10-FEB-2021, entry version 3. DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CAB0573616.1}; GN ORFNames=CIP107518_02190 {ECO:0000313|EMBL:CAB0573616.1}; OS Corynebacterium diphtheriae. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1717 {ECO:0000313|EMBL:CAB0573616.1, ECO:0000313|Proteomes:UP000476238}; RN [1] {ECO:0000313|EMBL:CAB0573616.1, ECO:0000313|Proteomes:UP000476238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP107518 {ECO:0000313|EMBL:CAB0573616.1}; RA Brisse S.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. CC {ECO:0000256|ARBA:ARBA00007553}. 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; CADDAJ010000037; CAB0573616.1; -; Genomic_DNA. DR Proteomes; UP000476238; Unassembled WGS sequence. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR CDD; cd06583; PGRP; 1. DR Gene3D; 3.40.80.10; -; 1. DR InterPro; IPR036505; Amidase/PGRP_sf. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR013207; LGFP. DR InterPro; IPR015510; PGRP. DR InterPro; IPR006619; PGRP_domain_met/bac. DR PANTHER; PTHR11022; PTHR11022; 1. DR Pfam; PF01510; Amidase_2; 1. DR Pfam; PF08310; LGFP; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00701; PGRP; 1. DR SUPFAM; SSF55846; SSF55846; 1. PE 3: Inferred from homology; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..587 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5026698559" FT DOMAIN 175..323 FT /note="PGRP" FT /evidence="ECO:0000259|SMART:SM00701" FT DOMAIN 189..352 FT /note="N-acetylmuramoyl-L-alanine amidase" FT /evidence="ECO:0000259|SMART:SM00644" FT REGION 375..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 386..400 FT /note="Pro-rich" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 587 AA; 61659 MW; 177A08B17E551091 CRC64; MAITLVGAAA VGVSTNSVLF TQGDAIAPIN PELTTSSLAD GNNVLVTDPA IATQGEGEGP KTVKEFHREQ PFSQFALTWN GERDIAAFVR GQRPDGTWTE WFDTEPLDYG SDNPNHKKGT DLIYIEPTTT VQVSISGVDL LGPDAANLDA VFIDGGTSDL PENGINLTAD SDGMPRVISR AGWGADESLR CSQPEYQDST AAIVIHHTAG SNNYSQKESP GIMRGIYKYH AQTLGWCDIG YHALADKYGN LFEGRYGGLN KSIVGAHAGG FNSNTWAISM MGNYDVVQPP QAMIKSVGEL AGWRAKVAGI DPKGYDTHYS EGSSYTFYPY GQAVRLPNIF AHRDVGNTSC PGQYGYAQMD NIRNIAKQKY DSIRSGSGAK APAAPSAPSN PAPAPAAPAA PSAPAATAGT NPIAQLSQGS TPANTGSLVG LAVAAATSLG LIGNLNNIGD VPVIGGLKLS QLQPIIGKIV ELLGNNDVSR VWRDVNSFAS AALGNARSPI AHYASATGTP IDYALFDNGI VISNPETGTN ALWGTIGDLW AQQGFEAGPL GLPTSSVFEV DGLQRVNFQH GYITFNPTTS AVDIQVQ //