ID A0A841DKK0_9ACTN Unreviewed; 639 AA.
AC A0A841DKK0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HDA44_002393 {ECO:0000313|EMBL:MBB5979052.1};
OS Kribbella solani.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=236067 {ECO:0000313|EMBL:MBB5979052.1, ECO:0000313|Proteomes:UP000558997};
RN [1] {ECO:0000313|EMBL:MBB5979052.1, ECO:0000313|Proteomes:UP000558997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17294 {ECO:0000313|EMBL:MBB5979052.1,
RC ECO:0000313|Proteomes:UP000558997};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
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:MBB5979052.1}.
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DR EMBL; JACHNF010000001; MBB5979052.1; -; Genomic_DNA.
DR RefSeq; WP_184833776.1; NZ_BAAAVN010000001.1.
DR AlphaFoldDB; A0A841DKK0; -.
DR Proteomes; UP000558997; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:TreeGrafter.
DR CDD; cd06583; PGRP; 1.
DR FunFam; 3.40.80.10:FF:000006; N-acetylmuramoyl-L-alanine amidase; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR051206; NAMLAA_amidase_2.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000558997};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..639
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038864383"
FT DOMAIN 260..397
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 639 AA; 68060 MW; E5103698F5646E5E CRC64;
MLRRPRILAA LGAVALPAAL VGVSLGGPPA AASPAPAPAA VAATAYQTAA AKYGVPESVL
LAVSYAESRW DDHAGAPSTT GGYGPMHLTG LGASEVADLS GKQKVATADS LQTLKKASEL
TGLDQSSLRN NVTDNINGGA AVLAAYQKSL GLPVGASTSP ADWYGAVASY AEAGDKVGAA
GFADDVYSIM ARGAARTTNT GQQIAMPALA VKPDKSQVDK LSLPAGVQPS KSDVECPVSL
GCEWLPAPYS QFGDGDYGNH DLANRPKTGK IDYIVIHDTE GHWQGVLNLV QDPTYVSWQY
TMRSSDGHTW QHVKAKDVAW HAGNWYVNQH SIGIEHEGFA PQGATWFTES LYRNSAKLVR
YLAVKNNIPL DRAHIIGHDQ VPGTLPSTVR GMHWDPGPYW DWEHYMDLVG APIWGKSVLP
VRAGSIVTIK PGFQGNVQVV DNCDTPGTPC KPQGTNFVYL RQAPDDNAPL VKDLGLHPDG
SNGTTDVSDM GSRAAAGSQY VVAQRQGDWV AVWYLGALGW FKSPASAPDA FVKPGLVVKP
KAGKTSVPVY GRAYPEQSAY PAGIPYQTVT PLQYTIGAGQ AYPVGDLNIE TDYYRAVTFD
GQPPTDHVQV IGKDRYYQIW FGHRMAYVRA ADVDVRPAI
//
