ID A0A011RLA8_9LACT Unreviewed; 441 AA.
AC A0A011RLA8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EXJ22638.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EXJ22638.1};
GN ORFNames=ADIAL_2224 {ECO:0000313|EMBL:EXJ22638.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22638.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ22638.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-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:EXJ22638.1}.
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DR EMBL; JANL01000042; EXJ22638.1; -; Genomic_DNA.
DR RefSeq; WP_034303437.1; NZ_JANL01000042.1.
DR AlphaFoldDB; A0A011RLA8; -.
DR STRING; 1229520.ADIAL_2224; -.
DR PATRIC; fig|1229520.3.peg.2169; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG3807; Bacteria.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000020164; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
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; 3.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EXJ22638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 36..99
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 105..167
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 177..242
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 441 AA; 48847 MW; DC22E2C490E29079 CRC64;
MKERDLHKPF SKRVFLFIVL ALFALMIGSL AALANENKVT VMTSTLNVRY GPGLSHEILT
QVHEEDSLNI LGEENQWYKV RLSNNNIGWV ASWLVENEEV SADTRANGRI SGNQVNIRQF
SSADSPVLGT VNMNEEYQIL YTEGDWVQIL YGGRVAWIHA NYIERLDSTV IAASSEETNG
HQIRIGMNPT NIRSSPDANA PLVQTVSSVE TYMVIGEENS WYEIELSDGS TAFVASWLTE
PVTDENEASA QSSQAAALPA THLSEATIVI DAGHGGHDPG AVAKTGFTEA DIALATSLKI
AENLRTAGAN VIMTRTDDTF VTLNDRVYYA HRAHADAFIS IHYDAVDIPN SMSGTTTYYY
SENERELADT INHYLIQNGP LRNNGVRHGN YFVLNSNHRP SILLELGYMN HDHDITLINT
AHYHQTIADA VYYGLSSYFS P
//
