ID A0A150MFW2_9BACI Unreviewed; 505 AA.
AC A0A150MFW2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KYD23430.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:KYD23430.1};
GN ORFNames=B4110_3184 {ECO:0000313|EMBL:KYD23430.1};
OS Parageobacillus toebii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD23430.1, ECO:0000313|Proteomes:UP000075324};
RN [1] {ECO:0000313|EMBL:KYD23430.1, ECO:0000313|Proteomes:UP000075324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4110 {ECO:0000313|EMBL:KYD23430.1,
RC ECO:0000313|Proteomes:UP000075324};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) 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:KYD23430.1}.
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DR EMBL; LQYW01000165; KYD23430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150MFW2; -.
DR PATRIC; fig|153151.4.peg.1602; -.
DR Proteomes; UP000075324; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; 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; IPR003029; S1_domain.
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; PS50126; S1; 1.
DR PROSITE; PS51781; SH3B; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KYD23430.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..505
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007564716"
FT DOMAIN 64..130
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 132..191
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 192..253
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 256..318
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 280..357
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 505 AA; 56463 MW; ED48EFEAFCBDD77E CRC64;
MLQPLRLLLV CSLMLFCYCS AAYAEMDSSA TSSRDNLQEI RDFHQPSPFN AKSSYASFST
ASTEKTIFAD VPADHWAKRE IEFLYERSII QGYNENGVLK FHPNENVTRA QAAKMIIKAL
GESEKPVTSA RFKDVPPSHW AVGWIERAVE KGIFKGYDDG TFQPNAPLKR SQMSKIIAIA
FKLPEPAVAK NQQIFRDIKP DYWAYPYIAK LYYHGISNGS DNQFMPESYI SRAQFSAFVA
RALNKDFRLS VNSPAIATGK VTADTLNVRS AGNANASVIG QLVRGTVVNV LEINGYWAKI
LYNGKTGYVH KSYLKLKNVS GNPVQGRIIV VDAGHGGTDP GTMKEKTYEK NIVLSVAKKL
KQKLESAGAK VIMTRESDVY KTLEERVQIA KNNYAELFVS IHVNSASPSA SGTETYYDTS
KNPNGYESYL LAKAIQQQIV SNASMKDRGV KDYNFYVVRN NNVPSVLIEL GFITNNSDYQ
KLTSDYYQDI FAQSIYNGIV QYYSQ
//
