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Database: UniProt
Entry: A0A2N5H496_9BACI
LinkDB: A0A2N5H496_9BACI
Original site: A0A2N5H496_9BACI 
ID   A0A2N5H496_9BACI        Unreviewed;       229 AA.
AC   A0A2N5H496;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:PLR99109.1};
GN   ORFNames=CVD19_03340 {ECO:0000313|EMBL:PLR99109.1};
OS   Bacillus sp. T33-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2054168 {ECO:0000313|EMBL:PLR99109.1, ECO:0000313|Proteomes:UP000235118};
RN   [1] {ECO:0000313|EMBL:PLR99109.1, ECO:0000313|Proteomes:UP000235118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T33-2 {ECO:0000313|EMBL:PLR99109.1,
RC   ECO:0000313|Proteomes:UP000235118};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) 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:PLR99109.1}.
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DR   EMBL; PGVB01000004; PLR99109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5H496; -.
DR   OrthoDB; 9763643at2; -.
DR   Proteomes; UP000235118; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
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; PF05036; SPOR; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235118}.
FT   DOMAIN          191..229
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   229 AA;  25708 MW;  20216ABACB9B77B6 CRC64;
     MKIMLDAGHG YNEPGKRSPD GMKEYEFNRV VANYAKQFLE GYENVTVYFA HSDDRVVPLQ
     ERTDKANQLN VDCYVSIHAN AYGNTWNDAG GIETYIYPTR PAEAAQLAAK IQRNLVASTG
     LKDRGVKTAD FHVLRETKMT AVLAECGFMT NPEEIKLLRS DSYRKTCADA ITRAVAEQYR
     LTKKPAPPPP PAGIGLYKVQ VGAFKDRNNA EALADRLRKD GYEPFIYFE
//
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