ID A0A2S7UUW1_9GAMM Unreviewed; 747 AA.
AC A0A2S7UUW1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BTO11_07455 {ECO:0000313|EMBL:PQJ53518.1};
OS Psychrosphaera saromensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Psychrosphaera.
OX NCBI_TaxID=716813 {ECO:0000313|EMBL:PQJ53518.1, ECO:0000313|Proteomes:UP000239007};
RN [1] {ECO:0000313|EMBL:PQJ53518.1, ECO:0000313|Proteomes:UP000239007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-48 {ECO:0000313|EMBL:PQJ53518.1,
RC ECO:0000313|Proteomes:UP000239007};
RA Yoshizawa S., Kogure K.;
RT "Diversity of luminous bacteria.";
RL Submitted (DEC-2016) 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:PQJ53518.1}.
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DR EMBL; MSCH01000003; PQJ53518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7UUW1; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000239007; 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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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 Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-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:UP000239007};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..747
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015536188"
FT DOMAIN 27..190
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 747 AA; 84784 MW; BA6C8BA9021D0099 CRC64;
MSKFIKRFFV ILFSVVLLNA CNSLPINKQI SVGQNARIQS LILHFTALNY ERSMYALKDS
GGVSAHYLIP EQQDSSYPNS NLEIIQLVDE NQRAWHAGVS YWDGRKNLND TSIGIEIVNV
PNCLHKPVVG YTHGGEYGAH RNCLFPNFEA EQIELLIELA QGILQRHPDI EPTKVIGHSD
ISPSRKNDPG PRFPWYQLYQ NGIGAWYEQE TVDKYLQDFS LVSPSINIVQ KALAFYGYNI
KETGILDSQT QDVLSAFQSH FLPTQVTGEL TPVTTATVFA LLDRYKQPRL EFLLKRYDKE
VDETLLISGR LSPRSNASKT NKHSINQTFY GAKGQGSLIL IHLDFASLNK LNVLINGKSL
DLKKARSVTT STNRTGIQLD ISNAVTNGTN VLKVTSKSDL SLLTIQMDSP TIIPATRWVD
RKLKNDLVNG LTQLEEDFEF SLVKNDKLIA HHAFGDSYLN NTLYLKQLTT FFTTQLAVLK
LVGDDRLRLD RPVSYYLSEY KGDGRGNRTI EHLLTHYSGY PSVENYLNGL MPDDELDSEN
IATRKSLPIQ WNKAIYNVPF YYGVNQKLNY SEFNDLVLRL VIEQVTNMTF EQFVENRILS
PLDLDSSIFR QVPNNNLYPV SLLTSQMKDI TILAQLFKSG GSYGKQNIFK PSSFTSWYQH
NSFWLIASEH NQINRLVGIQ ECHPYLTQNS HVAITEKGLV LVDDKLDISL VVYFPHAEKH
NVNQCGLSQQ QQDVLTKVFE IIYQAKS
//
