ID A0A0Q7QM08_9ACTN Unreviewed; 911 AA.
AC A0A0Q7QM08;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ASD11_10780 {ECO:0000313|EMBL:KQY59978.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY59978.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY59978.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY59978.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY59978.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY59978.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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:KQY59978.1}.
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DR EMBL; LMFJ01000001; KQY59978.1; -; Genomic_DNA.
DR RefSeq; WP_056286953.1; NZ_LMFJ01000001.1.
DR AlphaFoldDB; A0A0Q7QM08; -.
DR STRING; 1736550.ASD11_10780; -.
DR OrthoDB; 9773852at2; -.
DR Proteomes; UP000051970; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR InterPro; IPR013486; SpoIID/LytB.
DR InterPro; IPR013693; SpoIID/LytB_N.
DR NCBIfam; TIGR02669; SpoIID_LytB; 1.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF08486; SpoIID; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051970};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..911
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006320488"
FT DOMAIN 225..374
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 238..391
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 23..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 95628 MW; 6AF64EC6C0B9524D CRC64;
MAPCAVLSSA LLTVSLLAAP QAQAASGGGG DAGSAPAAVA PAAAPAVKTE QLEVPTTIRS
KAATPSPERQ GVGRADGSAA TVVAELEPTR VRSFRMVGVT WDADASLKDV KVEIRTREDG
TWTAWRGLEF DGHLDDGSPR DGTDADWIGE GADGVAARVS ASEGQPEGLR IATIDPGADA
NDAKPSEGDA TQSGALAPLS ASGVADGTAQ AVTAADTSPA YTPVPKIITR AQWGAAKPNS
CDTPRVGATT KGVVIHHTAG KNSYSKAESD NIMRADQSYH MKARGWCDIG YNFVVDKYGQ
IFEGRSGGYD RNVRAAHSGN DAVNTYTTGI SLQGNFDVAH VPDAMKNAVV RLVGWRLATT
FNPAKGTYSL GGKTLNRIAG HRNVVSTACP GKYGYAWLTA KGGLRDRVAN YIADYDTPTS
RLHDKLGDGT TGAVYSGEKV VAGGHRTVFD KADILQRTDV DTAYAVLSPV RNAYIARGRW
TDKLGWPIAS YTKTDTGGYQ KFQGGRITYT SATKKVSVTY GTTSTGSAGT TTKPTVNSAV
VPSSRTVTVK GHGYGHGIGM SQYGAEGAAR KGLSATSILR YYYPGTSLVK KSAKIRVLIS
ADTSPTVTVK SRSGLVYRNV TTNARRTLST KNTAGTTIEQ WRIEVDPAKK SRSILQYRVK
GTWSTYGKVA PWTGPAQIEA SSGALGLVLP NSSVASYRGA LRSVPPTAGS ADRNTVNVLG
LEEYTRGVVA AEVPSSWRAA TLRAQSVAAR TYGLRSLTSS RYYDICDTTS CQVYRGVGGE
TSSTNAAVST SAGLVLMYQG KPALAQFSSS SGGRSAAGSE PYLKDKVDAY DGWSGNANHD
WSTSLKASTI EKKYPSLGTL KRLTVTSRTG TGEDGGRVTR FALVGSRTTI RMSGPDARFG
LGLKSAWFSF S
//
