ID A0A0B0D073_9BACI Unreviewed; 462 AA.
AC A0A0B0D073;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LD39_12955 {ECO:0000313|EMBL:KHE69380.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE69380.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE69380.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE69380.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:KHE69380.1}.
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DR EMBL; JRNX01000432; KHE69380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0D073; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000030879; 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; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR001119; SLH_dom.
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; PF08239; SH3_3; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..462
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039054502"
FT DOMAIN 25..84
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 85..148
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 149..207
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 211..273
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 462 AA; 50762 MW; 59EF56DCC2FFDA96 CRC64;
MVRKIVPLLF ATFVLMLASF LPANVVHANS LSDIPDRSAD EINYLIDKGT VTGYPDGTYR
PKNSVTRQEA ATMVGRALGL NGTKRSTSFP DVSSSLYASG YIQSAYEQKI ITGYPDGTYQ
PRNEITRGEM AYLISKAFNL DETTGNKYSD VPNSGALSKA IDKVSTAGIA NGYPDGSFKP
QKSITREEYA LLVARGMNPK YKVDGEDLEV IDEKVVSTGI LNVRSGPGTN YSKIGQLTEG
AVIKIYKEIG SWVMFAYNGS TAYVHGAYIM DKPSNNGGHT IAIDAGHGDH DPGASDNGLV
EKEINLDVAK RVRDYLNNSN INVVMTRDDD TFLELDERVD YAVDHGADTF LSIHSNAFPN
NEDVSGVETY YSSAALSERA YDSYKLAHFI QNRVVEAMNA KDRGVKDIPY RVIHATPLPS
ALVELGFVTN DSDAYKLGSS YYRDRAAKAI YLGIVDYYNW KY
//
