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Database: UniProt
Entry: A0A1M6ZV20_9RHOB
LinkDB: A0A1M6ZV20_9RHOB
Original site: A0A1M6ZV20_9RHOB 
ID   A0A1M6ZV20_9RHOB        Unreviewed;       408 AA.
AC   A0A1M6ZV20;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN05444414_11163 {ECO:0000313|EMBL:SHL34264.1};
OS   Roseovarius marisflavi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL34264.1, ECO:0000313|Proteomes:UP000184191};
RN   [1] {ECO:0000313|EMBL:SHL34264.1, ECO:0000313|Proteomes:UP000184191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL34264.1,
RC   ECO:0000313|Proteomes:UP000184191};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001561};
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DR   EMBL; FRBN01000011; SHL34264.1; -; Genomic_DNA.
DR   RefSeq; WP_073198178.1; NZ_FRBN01000011.1.
DR   AlphaFoldDB; A0A1M6ZV20; -.
DR   STRING; 1054996.SAMN05444414_11163; -.
DR   Proteomes; UP000184191; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..408
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012048297"
FT   DOMAIN          238..393
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   408 AA;  43963 MW;  28869E60D2751EC3 CRC64;
     MMKWLMIVAM LCIAPGLRAQ EQGFSALARI DAEASRLADT RRGMELRLAL SQGVPYRVFT
     LDEPARLVMD FREIDWQGLS GAEFGDAERA TAVRLGQIRP GWSRMVVDLA GPHVLESAGL
     VVDRVTGAGD LRVVLGAADA GAFAAKAGTP DLPGWDLPNP EGALVAPERR VPGEGPLFVV
     LDPGHGGIDP GAQVGEVTEK DLMLQFALEL KEVLLRDGRF DVVLTRDADE FVPLERRVAL
     AHQGRADVFL SLHADALSGA RARGASVYTL SDSASDEASA ALAERHNRAD ILAGVDLSGK
     DDVVADILID LARQETQPRA ERLAKAVLAT LKAQDLPLLS RPQRHAGFSV LKAPDIPSVL
     LELGFLSSAR DLENLRDPAW RARMAGALRD AMLVWRREDG ARAGLVRQ
//
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