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Database: UniProt
Entry: A0A2C1K4V4_9BACI
LinkDB: A0A2C1K4V4_9BACI
Original site: A0A2C1K4V4_9BACI 
ID   A0A2C1K4V4_9BACI        Unreviewed;       237 AA.
AC   A0A2C1K4V4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase CwlD {ECO:0000313|EMBL:PGT81222.1};
GN   Name=cwlD {ECO:0000313|EMBL:PGT81222.1};
GN   ORFNames=COD11_18080 {ECO:0000313|EMBL:PGT81222.1};
OS   Bacillus sp. AFS040349.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT81222.1, ECO:0000313|Proteomes:UP000222674};
RN   [1] {ECO:0000313|EMBL:PGT81222.1, ECO:0000313|Proteomes:UP000222674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS040349 {ECO:0000313|EMBL:PGT81222.1,
RC   ECO:0000313|Proteomes:UP000222674};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-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:PGT81222.1}.
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DR   EMBL; NUMC01000084; PGT81222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1K4V4; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000222674; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR014234; Spore_CwlD.
DR   NCBIfam; TIGR02883; spore_cwlD; 1.
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.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222674};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..226
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   237 AA;  26820 MW;  5497E3229650F3AF CRC64;
     MDKKIKWLSF IGGFVLLLIL FQWQFSDNKS FESWNLPLTG KVIYIDPGHG GPDGGAVGSD
     TLEKDISLSI SLIIRDYLQE QGALVLLTRE EDVDLADEDT SGYSRRKAED LKKRVKIINE
     SEADLFLSIH LNAIPSAKWS GAQTFYSGRY IENENIAKYI QDELRRNLEN TERVAKPIDG
     VYLLKNLEKP GALVEVGFLS NPQEEKLLQT KSYQDKVAAS IYNGVLRYFS NEKNPPE
//
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