ID A0A168JSB8_9ACTN Unreviewed; 413 AA.
AC A0A168JSB8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:OAA21566.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:OAA21566.1};
GN ORFNames=UG55_105813 {ECO:0000313|EMBL:OAA21566.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA21566.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA21566.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA21566.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA21566.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA21566.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OAA21566.1}.
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DR EMBL; LRTK01000058; OAA21566.1; -; Genomic_DNA.
DR STRING; 683316.UG55_105813; -.
DR PATRIC; fig|683316.3.peg.4559; -.
DR OrthoDB; 9810670at2; -.
DR Proteomes; UP000077018; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OAA21566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077018}.
FT DOMAIN 275..389
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 44127 MW; 02005E73A94528A3 CRC64;
MKLLRLGDRD PSVAEARAAL IYLGFLPVAP RQTGTADGTA DLTATTPVPV XAPAHSSALG
GDGVEAAAAG DPADLFDRDL DNAVRAFQQS RGLSVDGVIG PDTFRAIEEA RRRLGDRLLY
YSVTHPFVGD DVAALQERLS NMGFDVGRAD GIFGARTDAA VRDFQRNRGL DPDGLCGPRT
LRELKRLERT VTGGRPDVLR ESVRLLARGP SLLGVVVAID PGHGGDDPGV TRGALCERDL
MADLASRLEA RLLASGLEAH LVHGPHESPA EAERAARANE IGADLLVSLH VDASGSEQAQ
GVSTYYYGHA RGSSAVGERF ATLVQREIVS RTDMVDCRAH PKTWELLRRT RMPAVQIDLG
YLTNAHDVAA LASTEFRAAV AEALLAATQR LFLPPEQDPP TGQLRVPRIA ART
//
