ID J2MKR4_9PSED Unreviewed; 402 AA.
AC J2MKR4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=PMI18_01151 {ECO:0000313|EMBL:EJM05536.1};
OS Pseudomonas sp. GM102.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144321 {ECO:0000313|EMBL:EJM05536.1, ECO:0000313|Proteomes:UP000007514};
RN [1] {ECO:0000313|EMBL:EJM05536.1, ECO:0000313|Proteomes:UP000007514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM102 {ECO:0000313|EMBL:EJM05536.1,
RC ECO:0000313|Proteomes:UP000007514};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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 -!- 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:EJM05536.1}.
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DR EMBL; AKJB01000020; EJM05536.1; -; Genomic_DNA.
DR RefSeq; WP_007896550.1; NZ_AKJB01000020.1.
DR AlphaFoldDB; J2MKR4; -.
DR PATRIC; fig|1144321.3.peg.1137; -.
DR Proteomes; UP000007514; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..402
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003751345"
FT DOMAIN 220..378
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 402 AA; 43641 MW; B30B26A5E8041710 CRC64;
MHRRHLLNLI LASAAFAFPF SASATQIRNA RLWRSDDKLR LVFDLSGPVQ YKTFSLSVPE
RLIIDLSGAN LSGDLSQLAL SNTVIRSIRS GHFGQGDTRI VLDLSGPVQL NSFLLAPQDG
QGHRLVLDLK PVAPLQIAAA PLDKREPVTD KAHPKRDIIV VVDPGHGGKD PGAVGAKGER
EKDVVLSIAQ LLAKRLKREK GFDVKLVRND DFFVPLRKRV EIARKHNADM FISVHADAAP
RLTASGASVY CLSEGGATSA TARFMAQREN GADLLGATSL LNLKDKDPML AGVILDMSMN
ATIAASLQLG STVLGSLAGI TTLHQKRVEQ AGFAVLKSPD VPSILVETGF ISNARDSQRL
VTARHQQAVA DGLFEGLQRY FQKNPPMNSY IAWQQEQKKT QA
//
