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Database: UniProt
Entry: A0A269W8C4_9BACL
LinkDB: A0A269W8C4_9BACL
Original site: A0A269W8C4_9BACL 
ID   A0A269W8C4_9BACL        Unreviewed;       461 AA.
AC   A0A269W8C4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:PAK53645.1};
GN   ORFNames=CHH75_10390 {ECO:0000313|EMBL:PAK53645.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK53645.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK53645.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK53645.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PAK53645.1}.
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DR   EMBL; NQLZ01000015; PAK53645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269W8C4; -.
DR   Proteomes; UP000215741; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR036582; Mao_N_sf.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   Pfam; PF07833; Cu_amine_oxidN1; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215741};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..461
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038529927"
FT   DOMAIN          348..455
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   461 AA;  49768 MW;  2392F62A86FA5C66 CRC64;
     MKKVGFLLFL VVMMIAFPRM ADASSYSAKI YLDGQELNLS SGVVVENQNG TVMVPIRVVS
     EQLGFRVSWT KATQTVTVQN SVKNVSMVIG SSYATIDGQR VQMTKAPVLR GGTTLVPLRF
     VSEQMGLQVR WDNQQKAVYL QSTGSGGEAP GSGNGSGTAA TVDGLSFNEN KLMVAVSGNA
     RANVSTLSNP DRIVIDLTNT RFSDGFGSNN NFNSVSQSGQ FTVSGYPDVK SVRYSLFNEN
     PMTVRIVVDL NYAKNYTVSG LENGSGILTV DLNTASAPNP GTGGKKLVVI DAGHGDQDPG
     AIGVTGKREK DFNLQMALKV QRLLQQEPNI DVVMTRSTDT FLELRERAKI ANDLKADVFI
     SIHTNSGPSS ASGTETYYYH ESDKALANAL HKEIVQAIGL RDRGVKYGNF HVIRETNMPG
     ALLEVGFLSN SNDESKLFDP ATQDRVAAAI VRGLKNYLQV N
//
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