ID A0A172ZEE6_9BACL Unreviewed; 464 AA.
AC A0A172ZEE6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ANF95647.1};
GN ORFNames=AR543_06295 {ECO:0000313|EMBL:ANF95647.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95647.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95647.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95647.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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DR EMBL; CP013023; ANF95647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A172ZEE6; -.
DR STRING; 1616788.AR543_06295; -.
DR KEGG; pbv:AR543_06295; -.
DR Proteomes; UP000078148; Chromosome.
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; 2.60.40.3500; -; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_sf.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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; PF11741; AMIN; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078148};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039331954"
FT DOMAIN 349..459
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 464 AA; 50921 MW; 3FBD814C87E68AFB CRC64;
MKKVIMLLLF SVMLVFLMPA HTNAAANQTR IVLDGQELSL PKDIGVVNMQ NNIMIPIRVV
AENLKFQVNW DQATQNVHIQ QGSNTVSLTV GKNTASVGNK TVKLGVAPQI IQNTVFVPLR
FVSEAMGLGV EWNNSDKIVT LASLVSSTPD APLPDSGSAT ATNWIHEINY VNNQLVVSLD
HEINPVITEL KNPERLVLDF PATNFGNMEN IPSPGAIARL DTSDSPNVKE IRYSLYQNNP
AQIRVVMELN NVSSVQYQPQ TTTGKFILDL DMVNDSGSTL PTDNGKKIVV IDAGHGGTDP
GTISITQKPE KNFTLALSLK VQALLKNEPD IEVIMTRETD VYPTRPERVK LANDLNADVF
VSIHANSVLA SPQAKGTETY YYQRESSKDL ANCIHEKLIQ ALGFTDRGIK NGSLQVIRET
TMAAVLLEIG FLSNKEEEEA MMSEDNQNKA AQAIVDGIKE YLEL
//