ID A0A0A1M6F0_9BACI Unreviewed; 919 AA.
AC A0A0A1M6F0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Sporulation-specific N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CEI80840.1};
GN Name=cwlC_1 {ECO:0000313|EMBL:CEI80840.1};
GN ORFNames=BN997_00650 {ECO:0000313|EMBL:CEI80840.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80840.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI80840.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI80840.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CDGG01000001; CEI80840.1; -; Genomic_DNA.
DR RefSeq; WP_052484876.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1M6F0; -.
DR STRING; 545501.BN997_00650; -.
DR OrthoDB; 9816557at2; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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; 6.
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:SF5; SPORULATION-SPECIFIC N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01471; PG_binding_1; 6.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF47090; PGBD-like; 6.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000040453}.
FT DOMAIN 800..911
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 101236 MW; D9F753DF9B2682A9 CRC64;
MRKKWIPFLL IILLIVSPFS SVSEVYAMDN KQSESSEENS ENVEDNKTGA EQDVLIDELE
SEELIFQLGD EDEIIQELKG NLTELGFATL DNPTNYFGLH TKKSVIAFQE FYNLEDTGIA
DEDTLEKIED ILSEGSFERD EHLEFSKPEE FEMEKEETEE GTEAEGEESP EAEEGTEAEG
EESPEAEEGT EAEGEESPEA EEGTEAEGEE SPEAEEGMEA EGEESPEAEE GTEAEGEESP
EAEEGTEAEG EESPEAEEGT EAEGEESPEA EEGMEAEGEE SPEAEEGTEA EGEESPEAEE
GTEAEGEESP EAEEGMEAEG EESPEAEEGT EAEGEESPEA EEGMEAEGEE SPEAEEGTEA
EGEDNSEADN TKDVQVQLFS TQSSNLQKGT SSEQAKKLKE DLKSLGYLTL PNPNNYYGVQ
TENAVKAFQK DNGLEQSGIA DRKTLDQIKK QLNRVPQKGT RTGEVKTLKE NLNRLGFTSF
PNPNNYFGVQ TEKGVREFQK QFGLTVNGMA DQATLAKIEE VLNSPLQSGK SNASSKELKE
NLKSLGYLNL ANPNNFYGVQ TANAVKAFQK DNGLAQSGIA DEVTLDKIKT EVNKVPQKGT
STEEVKNLKE DLNRLGFTSF PNPNNYFGVQ TERGVQNFQR QFGLTVNGIA DQATLAKIEE
VLNSSLQSGK SNASSKQLKE NLKRLGYLNL PNPNNFYGVQ TANAVKAFQK DNGLAQSGIA
DEITLIKIDQ EVKKLTNVKI FLDPGHGAHD PGGQGYGLNE KDVVLDIALE TERILTSKYQ
GVEVEMSRRS DVFVELTERA NHANRWGADY FVSFHNNAFN GSTGGFESYI YNGGVSQETR
NRQNDIHSYI SSRLNVSDRG QKSANFNVLR NTDMPAILIE YLFIDNFTEN ALLKSDSYKK
QLAQYTADAI AQSYNLKRR
//