ID A0A0B8ZYV2_BRELN Unreviewed; 282 AA.
AC A0A0B8ZYV2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:KHS51645.1};
GN ORFNames=AE0388_2195 {ECO:0000313|EMBL:KHS51645.1};
OS Brevibacterium linens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS51645.1, ECO:0000313|Proteomes:UP000031488};
RN [1] {ECO:0000313|EMBL:KHS51645.1, ECO:0000313|Proteomes:UP000031488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS51645.1,
RC ECO:0000313|Proteomes:UP000031488};
RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL Submitted (NOV-2014) 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:KHS51645.1}.
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DR EMBL; JTJZ01000020; KHS51645.1; -; Genomic_DNA.
DR RefSeq; WP_039210312.1; NZ_JTJZ01000020.1.
DR AlphaFoldDB; A0A0B8ZYV2; -.
DR PATRIC; fig|1703.6.peg.2093; -.
DR OrthoDB; 3268878at2; -.
DR Proteomes; UP000031488; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KHS51645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031488};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..282
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038485405"
FT DOMAIN 163..279
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 25..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 29110 MW; B9B78C87B29DF11A CRC64;
MRHRLLVPSL LASAALCLPG LAACSQGSDA SGPTTQAAET TGQSPSADKG ADGGEDAKSG
TASAKADDKD LEGKVIAVDP GHNGGNAKHP GEINRQVPDG RGGTKACNTT GTSTNSDYPE
ADFTWAVAKK LEKSLTDAGA EVVLSRKDNK GVGPCVDERG TFADDADLLV SIHANGSESS
SVKGYHVIVA DPGEDEKTEK ASVDLAKSVG TSMGEEFTPN KAYGKDAISR RPDLAGLNNA
SVPAVIVECG EMRNPSEAEL MESKSGQKKY ADALFDGIVD WF
//
