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Database: UniProt
Entry: E3E6Y0_PAEPS
LinkDB: E3E6Y0_PAEPS
Original site: E3E6Y0_PAEPS 
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
//
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