ID A0A086H0F6_STRSC Unreviewed; 658 AA.
AC A0A086H0F6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=IQ62_09455 {ECO:0000313|EMBL:KFG01124.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG01124.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG01124.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG01124.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KFG01124.1}.
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DR EMBL; JPPX01000076; KFG01124.1; -; Genomic_DNA.
DR RefSeq; WP_037692768.1; NZ_KL997412.1.
DR AlphaFoldDB; A0A086H0F6; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000028722; Unassembled WGS sequence.
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; IPR006311; TAT_signal.
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; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 286..423
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 658 AA; 70297 MW; 207AB0075286B3E0 CRC64;
MRGSPTDRRP TPYRGRTRRT AFAAAPAVLL LPLLGAAPPD SRPSSASARL QGAFAAAAAE
YGVPRDVLLG VSYLQSRWDA HGGAPSVTGG YGPMHLTDAR TALAEAPHHS EGTEDARGDD
SRAPLVAGAD LPEPAELPAR LKTLTRAAEL TGLPEETLRT DSEANVAGGA ALLAAAQREL
GARPSADPAD WYGAVARFSG ADDRATAAAY ANDVFAVIRD GARRVTDAGQ RVTLTAEPGL
DPGTGQLSRA GLRAAAAGAT ECPATVSCEW IPAPYEEFGD NDYGNHDLAD RPNSQPIRYI
VVHDTEGYWD TTLELVQDPT YVSWQYSLRS TDGHIAQHIK AKDVAWHAGN WYVNAGSIGL
EHEGFLASPD AWYTEAMYRA SARLVKYLSD KHGIPLDRQH ILGHDTVPGP TTATIPGMHT
DPGPYWDWRH YFELLGEPLG ATSGENSAMV TILPDYADNR PEFTGCATGG ARCAVHGSSA
VRLYSRPDAT SPLIKDIGLR PDGSASTIGV NDLGSRVSTG QQYAVAERQG DWTAIWYLGQ
KAWFQNPKGK PTAVGAAGMV VTPREGLADI PVYGRAYPEA AAYPAGVPAQ AVSPWPYKLL
KDQKYVTGGR VPGEYYYAVS FDTSGHRLVV GEDLYYEIQF GHRVAFVRAA DVRVLPAA
//
