ID E3E6Y0_PAEPS Unreviewed; 258 AA.
AC E3E6Y0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ADO58682.1};
GN Name=cwlD3 {ECO:0000313|EMBL:ADO58682.1};
GN ORFNames=PPSC2_22260 {ECO:0000313|EMBL:ADO58682.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58682.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO58682.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO58682.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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DR EMBL; CP002213; ADO58682.1; -; Genomic_DNA.
DR RefSeq; WP_013373246.1; NC_014622.2.
DR AlphaFoldDB; E3E6Y0; -.
DR STRING; 1406.LK13_09725; -.
DR KEGG; ppm:PPSC2_22260; -.
DR PATRIC; fig|886882.15.peg.4720; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_7_0_9; -.
DR OMA; QIRPVHH; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR014234; Spore_CwlD.
DR NCBIfam; TIGR02883; spore_cwlD; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..242
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 258 AA; 29162 MW; 3F3AA945C574C8C4 CRC64;
MQKNNRKKEV TLWIRYRTLQ KVLLGCCLAV LFIMLTLYEI PASRAWIHWS LPLTGKVIAI
DAGHGGPDGG AVSKEGVIEK DINLAIAFYL RDYLQQAGAV VVMTREDDRD LAQQETKGYS
RRKTEDLKQR VRMIEEQKAD LFLSIHMNSI PSSRWSGAQT FFVPNHADNE NLASLIQEEI
KRNLENTDRV AKTVNTVYLL KALKMPAALV EVGFLSHPEE ARRLSDENYQ RQVAASIYKG
ILRYSAGEKG TSSAPEVR
//