ID F2R5P4_STRVP Unreviewed; 639 AA.
AC F2R5P4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=SVEN_0268 {ECO:0000313|EMBL:CCA53555.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53555.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA53555.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA53555.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA53555.1; -; Genomic_DNA.
DR RefSeq; WP_015031475.1; NZ_JABVZO010000095.1.
DR AlphaFoldDB; F2R5P4; -.
DR STRING; 953739.SVEN_0268; -.
DR GeneID; 69862491; -.
DR KEGG; sve:SVEN_0268; -.
DR PATRIC; fig|953739.5.peg.5840; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_015278_1_0_11; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000006854; Chromosome.
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 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, ECO:0000313|EMBL:CCA53555.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..639
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003285041"
FT DOMAIN 269..405
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 85..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 67724 MW; F1F46C4C3EB09B75 CRC64;
MGVLASAALL FPLLSAAPQA GAQVPEAGAL QEQFARAATR HGVPESVLLA VSYLQSRWDA
HGGAPSVTGG YGPMHLTDAV TALAGSAPHH SEEAEDARGD SSRAVRSGAG TPVPAAASLP
ARLRTLERAS ALSGIPAEEL RTGTAANIEG GAALLAAAQR EAGLPASTDP GDWYGAVARY
SGADDSATAS TYANDVFDVI RAGESRRTDS GQVVTLPAAP SVEPATEQVA ALGLRRPAGG
PVECPRSVAC EWIPAPYEEF GDGDYGNHDK ANRPDSQSID YIVIHDTEAT WDVTLKLVQD
PTYVSWQYSL RSSDGHVAQH LRLKDVGWHA GNWFVNAKSV GLEHEGFLTA PDSWYTEAMY
RTSARLVRYL AARYGIPLDR QHILGHDNVP GTVTSSIKGM HTDPGPYWDW AHYFRLLGRP
ITPSAGPRAE VVTIRPEYGA NRPVYTGCVT AGEACAPHGS GAVRLHTAPS ADAPLVKDIG
LRPGGQDSTT GVNDTGARAS TGQSFAVAER RGDWTAVWYL GQMAWFHNPV KAPTAVNARG
LVLTPREGLA SVPVYGRAYP EAAAYPAGVP VQAVSPLPYR LLAGQRYVVG GRTPGEYFFA
PVFDSSGHKV VRGQEEYYQI QFGHRVAFVK AADVRVSPS
//
