ID   A0A1I3W791_HALDA        Unreviewed;       651 AA.
AC   A0A1I3W791;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SFK03534.1};
GN   ORFNames=SAMN04487936_106239 {ECO:0000313|EMBL:SFK03534.1};
OS   Halobacillus dabanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=240302 {ECO:0000313|EMBL:SFK03534.1, ECO:0000313|Proteomes:UP000183557};
RN   [1] {ECO:0000313|EMBL:SFK03534.1, ECO:0000313|Proteomes:UP000183557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFK03534.1,
RC   ECO:0000313|Proteomes:UP000183557};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOSB01000006; SFK03534.1; -; Genomic_DNA.
DR   RefSeq; WP_075036842.1; NZ_FOSB01000006.1.
DR   AlphaFoldDB; A0A1I3W791; -.
DR   Proteomes; UP000183557; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
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; 3.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   PANTHER; PTHR30404:SF5; AUTOLYSIN PH-RELATED; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF05036; SPOR; 3.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 3.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51724; SPOR; 3.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          193..272
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   DOMAIN          285..364
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   DOMAIN          375..454
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   REGION          452..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          623..650
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   651 AA;  71944 MW;  76B580940B2B5D42 CRC64;
     MKTVVIDAGH GGSDPGATYR GFQEKTFNLS IALNVQRILS QNYQVSIIMT RTTDTSLSLT
     ARTNIANRNN ADFFLSIHNN AAGGSGFETY IYNGPLSPNT QTYQNIIHES TYNAIGNKYN
     VRDRGKKRAN LHVTRETDMS SLLIEVLFVD NDGDLALLRN SNFINDVSRG IAEGVADALN
     LPRKSQPDPQ PSPGDDSLYR VIAGSFRNRE NAEQRIEALS QEGIPGFVVP TTISGTQYFR
     VQTGAFSNEA NAKEQVERLK RIGITSAFII RGEESSPAPD PEPEKPTDGL YRVIAGSFRN
     RENAEQRVQS LSREGITSFI VQTDISGVTY YRVQTGAFSE QENAQELVDR LKSLGITDAF
     ITREGETQPD PDPGTPSDGL YRVIAGSFRN RENAEKRIEL LEREGIAGFI VQAEISGVTY
     YRVQTGAFSE KENAEEQVER LKAIGIPDAF ILQGEDAPPP GDPDPDPEPP ADDGYTIQGD
     TYLTACQMDD YVKTVNPDAP ELGRFYVQYG EAYGIRGDVA FAQAIHETDY FRFTGLVDAE
     QNNYAGIGAT GPGNPGAEFS TPEEGVHAHI QHLYAYTSTE PIPSRFEKVD PRFDLVTRGI
     ASSWSGLNGR WAVPGDNYGQ LILQIHERNI EHALEEMEEQ REQLNDVLEE L
//