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Database: UniProt
Entry: A0A0R1HJS4_9LACO
LinkDB: A0A0R1HJS4_9LACO
Original site: A0A0R1HJS4_9LACO 
ID   A0A0R1HJS4_9LACO        Unreviewed;       255 AA.
AC   A0A0R1HJS4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Cell wall amidase lyth {ECO:0000313|EMBL:KRK46656.1};
GN   ORFNames=FC66_GL000280 {ECO:0000313|EMBL:KRK46656.1};
OS   Dellaglioa algida DSM 15638.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Dellaglioa.
OX   NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK46656.1, ECO:0000313|Proteomes:UP000051450};
RN   [1] {ECO:0000313|EMBL:KRK46656.1, ECO:0000313|Proteomes:UP000051450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK46656.1,
RC   ECO:0000313|Proteomes:UP000051450};
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:KRK46656.1}.
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DR   EMBL; AZDI01000001; KRK46656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1HJS4; -.
DR   STRING; 1423719.FC66_GL000280; -.
DR   PATRIC; fig|1423719.4.peg.282; -.
DR   Proteomes; UP000051450; 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   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   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051450};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          6..69
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   255 AA;  28400 MW;  EDDDD97ECDBAC37B CRC64;
     MKTMSYLGET VVESDNINVR TGPSTSFKVT DTLKKGERIS IIREKNNWSY VLLPDDKKGW
     VANWLLSKKN ATVTKLSEAT IVLDPGHGGN DSGALSIKKK QEKIYTLQMA TRVANLLKAR
     GANVLLTRDS DSYVGLTPRA KLAESNNADA FISFHFDSSP NDNEATGLTS YYYKKSTDFA
     LASALNVELN NTGLNNRGTE FGDFLVLREN TQPSVLLELG YINTKYDFKL IQNDNFQEKT
     AESIVNGLDN YFKNK
//
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