ID K0Z773_9ACTN Unreviewed; 283 AA.
AC K0Z773;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HMPREF9451_01799 {ECO:0000313|EMBL:EJZ83280.1};
OS Slackia piriformis YIT 12062.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=742818 {ECO:0000313|EMBL:EJZ83280.1, ECO:0000313|Proteomes:UP000006069};
RN [1] {ECO:0000313|EMBL:EJZ83280.1, ECO:0000313|Proteomes:UP000006069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12062 {ECO:0000313|EMBL:EJZ83280.1,
RC ECO:0000313|Proteomes:UP000006069};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Slackia piriformis YIT 12062.";
RL Submitted (AUG-2012) 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};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EJZ83280.1}.
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DR EMBL; ADMD01000009; EJZ83280.1; -; Genomic_DNA.
DR RefSeq; WP_009139976.1; NZ_JH815199.1.
DR AlphaFoldDB; K0Z773; -.
DR PATRIC; fig|742818.3.peg.1902; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_085720_0_0_11; -.
DR InParanoid; K0Z773; -.
DR Proteomes; UP000006069; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006069}.
FT DOMAIN 107..264
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 283 AA; 30411 MW; 2A7BC77B308E1838 CRC64;
MIRMNAAQQG GVAHRILPRA GRAIAACSLF GAMAFGVSDA YGGDARTSFD GDEGGRSVFA
GALRQASPAL FKMLDEWSSF LEEAAAARPS AEELRASLAL SEDYRGSFSH GPKPAEYQKY
IVLHDTEGSA DAASVISWWD ASGNGVAAHF IVNKDGSIVQ CVSLDEIAHH AGFGDTGHNA
AFGVEDESRD DKVGTTPIGD WASDYGMNSY SIGIEMVHRG GEGDYPEEQL QSLDALIAYI
DAYYGFKSEI IDHKAWRTGN SDTSPEFASY FANYKECRAH EAP
//
