ID A0A0R1ZM13_9LACO Unreviewed; 438 AA.
AC A0A0R1ZM13;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KRM56080.1};
GN ORFNames=FC18_GL000867 {ECO:0000313|EMBL:KRM56080.1};
OS Lacticaseibacillus sharpeae JCM 1186 = DSM 20505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM56080.1, ECO:0000313|Proteomes:UP000051679};
RN [1] {ECO:0000313|EMBL:KRM56080.1, ECO:0000313|Proteomes:UP000051679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM56080.1,
RC ECO:0000313|Proteomes:UP000051679};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM56080.1}.
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DR EMBL; AYYO01000010; KRM56080.1; -; Genomic_DNA.
DR RefSeq; WP_054676311.1; NZ_BBAC01000002.1.
DR AlphaFoldDB; A0A0R1ZM13; -.
DR STRING; 1291052.FC18_GL000867; -.
DR PATRIC; fig|1291052.5.peg.883; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000051679; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051679};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 33..95
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 102..163
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 182..244
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 438 AA; 46663 MW; B0322E6495D12F82 CRC64;
MKKSLHLKKL PLFIVTVALL GISLATTTVL AGTKTLTVNA SVLNIRRGPG LAYDVMGQSQ
SGAKLNVIAE RNSWYEVRLA GNKVGWVASW LVNSDDANTN AAKVARVTSR VNVRKYASTS
ATLLGALNPG ASVKVVYSQG DWSQIVYSDT AAWVSTKYLE LTGQTTTVTS TQTAVSKANT
ATQIKVKTNT NTHLRQAGGI NAAIVENLSK GAELTVLNQD GDWFHVRAAD GKTGYIANWV
VSTPSDGKSS KAATSLNEAT IVLDAGHGGS DPGASSTAGE KEKTYTLETV DAIATQLRAA
GANVVLTRSS DQYVDLAQRP VIAANVNADA FISIHFDSSP ESNTAEGHTT YYYTKSKDYT
LATYLSTSLA NLSTASRGTS FGNFEVIRDN KQPSVLIELG YINDDDDFQK LSSSTYQHQA
AIDIVNGLTK YFAAGNHR
//
