ID A0A150N4G6_9BACI Unreviewed; 466 AA.
AC A0A150N4G6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KYD31620.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:KYD31620.1};
GN ORFNames=B4110_3335 {ECO:0000313|EMBL:KYD31620.1};
OS Parageobacillus toebii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD31620.1, ECO:0000313|Proteomes:UP000075324};
RN [1] {ECO:0000313|EMBL:KYD31620.1, ECO:0000313|Proteomes:UP000075324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4110 {ECO:0000313|EMBL:KYD31620.1,
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:KYD31620.1}.
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DR EMBL; LQYW01000033; KYD31620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150N4G6; -.
DR PATRIC; fig|153151.4.peg.2205; -.
DR Proteomes; UP000075324; 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; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR017293; N-acetylmuramoyl-L-ala_amidase.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR036028; SH3-like_dom_sf.
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; 3.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KYD31620.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 116..178
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 184..247
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 466 AA; 51231 MW; 2206FCA154B99AD3 CRC64;
MCANDIVDKL ETTGEGMRMR RGIWLALLFC LLWLAAAAWP VGAKGEKEME ETKRLAVVTA
DQVNVRQGPG VPYRPLANVH RGEAYRLIEV KDGWVNIEWK PNRTGWIAAR YVALAKETAI
VQENRLRLRQ EPSRDGRIIG HLARGETVWI IKEDGEWTEV IADGAIGWVS SAYLTAARES
SISHQTGIVN ASSLNVRAEP SLKAARVGRL VRGEEVEIVE KKPGWYKIAS QTGLDGWVSS
AYVQVKGGQA NEKEAEAPQS ADHSLLSAIA PSDSRLYVDS WTRGPVQALA GKTIVLDAGH
GGKDGGAQSV DGIKEKELTL ETAKLLKNKL QSYGARVVLT RSSDEYVPLS ARVAAARLYQ
ADAFISLHYD SAADPDASGI TIYYYDRFAD YELAQSFQGL FRQLSALPFR GIAFGDYYVL
RENEKPSVLL ELGYLSNRSD AAVVATNGYQ EAVTTAIVNA VRHYFQ
//
