ID A0L9I7_MAGMM Unreviewed; 416 AA.
AC A0L9I7;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Mmc1_2129 {ECO:0000313|EMBL:ABK44630.1};
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK44630.1, ECO:0000313|Proteomes:UP000002586};
RN [1] {ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2] {ECO:0000313|EMBL:ABK44630.1, ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=22581902;
RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA Bowser S.S., Dean A.J., Beveridge T.J.;
RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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};
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; CP000471; ABK44630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0L9I7; -.
DR STRING; 156889.Mmc1_2129; -.
DR KEGG; mgm:Mmc1_2129; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_3_5; -.
DR Proteomes; UP000002586; Chromosome.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABK44630.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586}.
FT DOMAIN 246..406
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 416 AA; 46748 MW; 9A1045A99AB8EAF4 CRC64;
MLTDDNMELM DIHRRLNRLS DVNRRQLLQL LALTSGGMLL PNLAEASLGP NQIKDIRVWT
APDHSRVVFD LERPVKHTLF RLKNPDRVVL DIENAILSQS TSHLRIKDPV VRAFRMGIPR
PDTTRAVFEL NEEVRPRSFL LKATKDRGPR LVIDLYRKGE LERQARLERE YDPFRNRTPV
RENMVVVIDP GHGGEDPGAT GPSGVREKDV VLTVAKKLAA MVNATPGYEA KLTREGDYYV
SLKKRVGIAR QYDPDLFMSL HADSFRIRSA RGTSVYCLSE QGKPTPDRAI KDLVERENST
DLVGGVNLGK VVDPEVAGIL MDLSQRDSLN RSLVLGRNLL DSLDAMPQVR LHYRNVKQAG
FAVLKAPDIP SVLVELAFLS NPNEEMMMKK ESYQATLAAG LLKGVERFAK ASREIS
//
