ID A0A0R1Q666_9LACO Unreviewed; 438 AA.
AC A0A0R1Q666;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KRL37818.1};
GN ORFNames=FD01_GL002775 {ECO:0000313|EMBL:KRL37818.1};
OS Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL37818.1, ECO:0000313|Proteomes:UP000051790};
RN [1] {ECO:0000313|EMBL:KRL37818.1, ECO:0000313|Proteomes:UP000051790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL37818.1,
RC ECO:0000313|Proteomes:UP000051790};
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:KRL37818.1}.
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DR EMBL; AZEU01000313; KRL37818.1; -; Genomic_DNA.
DR RefSeq; WP_056965134.1; NZ_AZEU01000313.1.
DR AlphaFoldDB; A0A0R1Q666; -.
DR PATRIC; fig|1423769.4.peg.2995; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000051790; 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 InterPro; IPR010916; TonB_box_CS.
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.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051790};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 32..94
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 97..162
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 179..245
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 438 AA; 46648 MW; 145432072A76E8AA CRC64;
MKFKQLHRWP LMILLAVLIG ISAATTVVLA NNNTLTVTAS VVNVRFGPGL SYNTMGQVQK
GGNLTILKKQ NSWYQVRLAG NRVGWVASWL VHEDAATTSA AKVARTTTNV NVRQYASSSA
KQLGTLSSGS TVSVLYQSNG WSQIQYNNTA AWVDSSLLQL TGATTTINPT QTAIATAKAT
TPTLKATTTL AANVRQTAGL NAAVVTRIAK GATVTVLSQS GDWYHVRTAD GKTGYIASWI
LSMPGASTNK AATKLSEATI VIDPGHGGND TGALSTSGKY EKTYTLQMAK AVGAKLEAAG
AKVVYTRSTD TYVDLAPRPV VAKKVHADAF ISFHFDSTPN ANTASGFTSY YYNASKDKAL
ATNLNKALGS NLSLTNRGIA FGNYEVLRDN DQPSVLLEMG YINDDHDFKF IESSTYQQTV
AADIVNGMNA YFAAGNHQ
//
