ID A0A0M0L7J2_9BACI Unreviewed; 475 AA.
AC A0A0M0L7J2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMD01_09910 {ECO:0000313|EMBL:KOO46658.1};
OS Priestia koreensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO46658.1, ECO:0000313|Proteomes:UP000037558};
RN [1] {ECO:0000313|Proteomes:UP000037558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14210 dsm16467.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:KOO46658.1}.
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DR EMBL; LILC01000013; KOO46658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0L7J2; -.
DR STRING; 284581.AMD01_09910; -.
DR PATRIC; fig|284581.3.peg.2061; -.
DR Proteomes; UP000037558; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR001119; SLH_dom.
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; PF08239; SH3_3; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 1.
DR PROSITE; PS51272; SLH; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037558};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 12..70
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 71..134
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 184..248
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 249..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51466 MW; 984118A8B131D332 CRC64;
MLGTFSNLTV KAETTFVDVP NNHRAAKEVN FLAEGGILNT SSNRLNPDET ITRAEAVSII
GRATQLDGTQ RQTKFSDVQA SAKEAGYIQS AYEKHYLSGY ADGTFKPEQK VSRGEMALLI
SRAFNYGATN TGSANQALLS KKISTGLGNG QFGGNELIKR ADYAVFIARA INSSFRSGYT
KAFPQQGKVT ASALTVRTGP STQYGKIASV GNGKMLKIDH FVGTWAEVVD DKNSFFGFVS
SSYLAITPTN GGGATDTNQP DPNPTTPTTP SPVLNPLANK KIIIDPGHGG KDTGAIGNGM
NEKDIVLDVG LKVQQVLNRM SVPSYLTRST NVFIELKDRP IIAKQQKGDI FVSIHINSSA
KPESGTGIET HYYAGATNPY NAQSKLLAQC IQKRLVEEWK LADRGIHPTN LYVNKYNSMP
AVLAELGFIN NSTDAAKLKS DYWRQKDAEA IVLGILDYYK ANKIDVSSLY PLVRQ
//
