ID   D4CFT1_9CLOT            Unreviewed;       527 AA.
AC   D4CFT1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EFE11448.1};
GN   ORFNames=CLOM621_08302 {ECO:0000313|EMBL:EFE11448.1};
OS   Clostridium sp. M62/1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=411486 {ECO:0000313|EMBL:EFE11448.1, ECO:0000313|Proteomes:UP000004936};
RN   [1] {ECO:0000313|EMBL:EFE11448.1, ECO:0000313|Proteomes:UP000004936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M62/1 {ECO:0000313|EMBL:EFE11448.1,
RC   ECO:0000313|Proteomes:UP000004936};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) 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:EFE11448.1}.
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DR   EMBL; ACFX02000036; EFE11448.1; -; Genomic_DNA.
DR   RefSeq; WP_008398590.1; NZ_GG730315.1.
DR   AlphaFoldDB; D4CFT1; -.
DR   HOGENOM; CLU_536065_0_0_9; -.
DR   OrthoDB; 9794294at2; -.
DR   Proteomes; UP000004936; 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   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR041219; Phage_lysozyme2.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF18013; Phage_lysozyme2; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   4: Predicted;
FT   DOMAIN          375..449
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
SQ   SEQUENCE   527 AA;  56583 MW;  B61382282516924F CRC64;
     MSLIGKNNEE KIWNFLTGKG LNSYGAAGLM GNLFAESGLN PHNLQNTYEK KLGYTDDDYT
     DAVDSGKYTG FVHDSAGYGL AQWTFWSRKE ALLNYVKAAG ASIGDLETQL GFLWKELAES
     YTAVLAVLKK ATSVRQASDA VLLKYEQPKD QSASVQTKRA SYGQTYFDKY ATKTTNDTQG
     GKTMSNSSLV DCTVYSPNHS GKRTHSIDRL TPHCVVGQLS AETIGACFPK GRDASCNYGI
     GYDGRVCLIV DECNRSWCSS SNANDQRAIT IECASDKAEP YAMKSAVYEK LIKLCADICK
     RNGKTKVLWL GSKEKALAYE PKANEIVLTA HRWFANKSCP GDWLYSRYGE LADRINALLG
     STDSGNSGGN NTPSGGSGVK YYVQTGAYKQ KANADAQLKK VKAAGFDAIL KQSGGFYKVQ
     TGAYSKKENA DAEVKKLKAK GFDAIVTTDG GNAAGSASSE IKVGDVVQFS GGPHYGSTAA
     STAAGSPKAG PAKVTRIVKG AKHPYHIVHT DSQSNVYGWV DAANVSK
//