ID A0A0A3IFA5_9BACI Unreviewed; 513 AA.
AC A0A0A3IFA5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KGR83446.1};
GN ORFNames=CD32_16590 {ECO:0000313|EMBL:KGR83446.1};
OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR83446.1, ECO:0000313|Proteomes:UP000030437};
RN [1] {ECO:0000313|EMBL:KGR83446.1, ECO:0000313|Proteomes:UP000030437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR83446.1,
RC ECO:0000313|Proteomes:UP000030437};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL Submitted (FEB-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:KGR83446.1}.
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DR EMBL; JPVP01000058; KGR83446.1; -; Genomic_DNA.
DR RefSeq; WP_036156631.1; NZ_JPVP01000058.1.
DR AlphaFoldDB; A0A0A3IFA5; -.
DR STRING; 1220589.CD32_16590; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR eggNOG; COG4991; Bacteria.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000030437; 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; 4.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR017293; N-acetylmuramoyl-L-ala_amidase.
DR InterPro; IPR003646; SH3-like_bac-type.
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; 4.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 4.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030437};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002001700"
FT DOMAIN 27..88
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 94..159
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 175..238
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 251..313
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 513 AA; 56571 MW; 3FEE4DB5A0E708FF CRC64;
MRQAFHIIIV CMLIFSIALP TTSNAAGDDL VVAAEVLNLR EGPGLSYPIL LKLKEGDTVS
TIEYEGDWIH VKAGNTEGWI AGWMTKANVQ TESKQTQKVI ISQVDHLNVR AEPSLSSTVL
TQLPSGNEAT YIKSQNDWIQ IHYGTTTGWV SSQYVTVKEL SKAAAEEIAE APSEGNMFTV
TVDAVNVRKK ADLTSKRVGS AYRGEQFKVL EQSNNWVHIQ YKNNTEGWIY KFYGSFGEQA
PSSTSKASPS DESVTIIYEG TNLRQEASTS SAIVYRANAG ETYRILEEQG DWYKVSVNGN
KTAYVANWVV SGTDTKQQSP AVKRTAAERK NGTLKGVTIV IDAGHGGNDH GTTGSRGTDE
KGITLKTAEM LKSKLRAAGA DVIMTRESDV YVDLRKRVAI SHQVEADAFI SLHYDATENS
AVSGVTTYYL NSNQQELAKY VHAKLAKKVS LRDRGVQPGN YLVLRENRQK AILIELGFLS
NPSEERSITT DYYREQATLG IYEGILDYFD SQL
//
