ID A0A0G3AM08_9ACTN Unreviewed; 656 AA.
AC A0A0G3AM08;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ABB07_34600 {ECO:0000313|EMBL:AKJ15006.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ15006.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ15006.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP011497; AKJ15006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3AM08; -.
DR STRING; 665007.ABB07_34600; -.
DR PATRIC; fig|665007.5.peg.7313; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 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 PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..656
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005183722"
FT DOMAIN 286..423
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 656 AA; 70385 MW; 5FF1DD854F3BF887 CRC64;
MRGSATDSAS APGPRHLRRA AGPLASAALL LPLLGAAPAQ GATDASAGRL QHAFATAAAE
YHVPQSVLLA VSYLQSRWDW HAGAPSVSGG YGPMHLTDAR TAIATTEHYA EGTEDARGDA
ARAAVHPEIQ VPADSALPAR LKTLPKAARL TGRPAEELRT DPAANVAGGA ALLAAAQQEL
GEPLSADPAD WYGAVARFSG ADDTATARAY ADDVYDVLRT GEERVTDDGQ LVALAAQPRL
TADTAQLRRA GLGTLPTDGV ECPNSVSCEA VWAPYAQFGS NDYGNHDLGD RPVSQSIKYI
VIHDTEGAWD GVLNLIQDPA YVSWNYTIRS TDGLIAQHVK AKDVAWHAGN WYVNAKSVGI
EHEGFLANPD AWYTEAMYRS SARLVRYLAA KYGIPLDRQH ILGHDNVPGP TTSTIPGMHT
DPGPYWDWRH YFQLLGHPFK RTAGKRGGLV TILPDYAANQ PVYMGCTTSG EPCTAHGSSE
VRLYSDHDVN APLIKDIGLK KDPTEDVNDL SSRVSTGQQY AVADRWGDWT AIWYLGQKAW
FRNPPGEPAA VPAKGLVITP KEGLTSIPVY GRAYPEQAAY PAGVPPQSVV PLPYTIPAGQ
RYVVGDEVPG EYYYSVTFTT DSHRVVVGKD LYYEIQYGHR VGFVRAADVT LEGSAS
//
