ID A0A0M2SL27_9BACI Unreviewed; 501 AA.
AC A0A0M2SL27;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KKK33305.1};
GN ORFNames=WQ57_24455 {ECO:0000313|EMBL:KKK33305.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK33305.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK33305.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK33305.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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:KKK33305.1}.
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; LAYY01000101; KKK33305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2SL27; -.
DR PATRIC; fig|1408103.3.peg.5276; -.
DR Proteomes; UP000034166; 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:UP000034166};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 21..83
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 93..155
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 168..231
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 241..305
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 501 AA; 53371 MW; F7B1B1EF251E25DA CRC64;
MAEWFTKKEG AAAVAPSAGA SGTGIVAADS LRVRSGPGTS YASTGSLRNG QSVTVLNTNG
SWAKIRHGSL EGWVSKDYLN MNGSRQQSVP AAGNDAIAAA DNLNVRVSPA LNARVIGKLA
KGTKVKVQSQ ENGWAKIIYQ GQAAYVSGQY LSFTSSPLKT GSAASRPAGE ATVTASSLYV
RDSGSLNGKV VGQVSRGEKF RILAEKDNWV KIEYKPGRTG WAAGWFFEKK ASSPAPSANS
VKNQSVTVLH NGTNIRKGAG VHTSVVQRAN QGDSFKVVSL YGDWYQISLA NGGTGYIAGW
LVSLNGNQAV QIKKPGAGIH MKNKTVVIDP GHGGRDGGTV GARGTLEKHL NLATARLLYD
KLKAAGTNVV MTRNGDTYLS LSSRVSASHY HNADAFISLH YDSIADRSVR GMTTYYYNSS
HRTLSTEVHS SVSSRTSLRD RGVRQGDYHV LRENQRPSTL LELGYLSNPT EEMLVSTPQY
QEAVAAGIFE GLAKYFKGSG Q
//
