ID A0A0R1K817_9LACO Unreviewed; 536 AA.
AC A0A0R1K817;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cell wall-associated hydrolase {ECO:0000313|EMBL:KRK77395.1};
GN ORFNames=FD30_GL001910 {ECO:0000313|EMBL:KRK77395.1};
OS Levilactobacillus namurensis DSM 19117.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77395.1, ECO:0000313|Proteomes:UP000051162};
RN [1] {ECO:0000313|EMBL:KRK77395.1, ECO:0000313|Proteomes:UP000051162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77395.1,
RC ECO:0000313|Proteomes:UP000051162};
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 peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:KRK77395.1}.
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DR EMBL; AZDT01000006; KRK77395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1K817; -.
DR STRING; 1423773.FD30_GL001910; -.
DR PATRIC; fig|1423773.3.peg.1956; -.
DR Proteomes; UP000051162; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR47053; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR PANTHER; PTHR47053:SF1; MUREIN DD-ENDOPEPTIDASE MEPH-RELATED; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF00877; NLPC_P60; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KRK77395.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..536
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038814653"
FT DOMAIN 34..79
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 85..128
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 415..536
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 173..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 54869 MW; C8A0F8207D799489 CRC64;
MKMSTSQRKT KVAVGVVGAL GALAAGAQLT ASANSIQVQA GDTVWGLSQK YGVSIQTLEE
QNSLDTNTDL IFIGQRLQVT KNNQKTYTIK SGDTLWDLAQ HYHTTVAALQ KANHLTGAML
SVGQKLTIPT TGDVTGTQAE SVAPVISQKI TKQASAFQAQ ILAQQQAAAS QQQQRQSSAS
TNSAATQSTT TTDQSATATT SAAASASSSS TVAKTYQHAE SATPTSRAQT TTAQRQSTSQ
QPATSKAAQS SSVTSAQSAT TATTSSAATS QATAKAPSTS QQSGSAQSQS QAVATTRQAT
VKTKQSSTQS QASQATQTSQ TPVTRATTTK TVKQAPKAVK TPRRAKVSAY RASVSSSTTS
RVSQPQQQVT AASSSSTASA TSSRATSAVA QPKKSTTPTT AASASSTTTK KNTAGLTSGS
VTGLALKLAS ANIPYVWGGS SLSGMDCSGF VAYVYQHASG ISLPHSTVAQ ESRVTTHSVA
SAQPGDLLFW GSKGATYHDA IYLGNGEFVA APAPGQNVSV QTISKYFMPS FAGTLK
//
