ID F9VFM2_LACGL Unreviewed; 517 AA.
AC F9VFM2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=N-acetylmuramidase {ECO:0000313|EMBL:BAK61123.1};
GN OrderedLocusNames=LCGL_1663 {ECO:0000313|EMBL:BAK61123.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK61123.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK61123.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK61123.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009333; BAK61123.1; -; Genomic_DNA.
DR AlphaFoldDB; F9VFM2; -.
DR STRING; 420890.LCGL_1663; -.
DR KEGG; lgv:LCGL_1663; -.
DR PATRIC; fig|420890.5.peg.1638; -.
DR eggNOG; COG1705; Bacteria.
DR eggNOG; COG2374; Bacteria.
DR eggNOG; COG3942; Bacteria.
DR HOGENOM; CLU_017855_4_1_9; -.
DR Proteomes; UP000008520; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50911; CHAP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003389315"
FT DOMAIN 385..514
FT /note="Peptidase C51"
FT /evidence="ECO:0000259|PROSITE:PS50911"
FT REGION 65..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 55643 MW; 8F0285748A987A33 CRC64;
MKLTMAEKKY KHMKVKERKA LPKVALSAAA VLGVAAFGAN AHADSATSTA SDIKAVTNLD
TLALNSEENM VEAGDNGQLE NSETENSTDP TNPTDPTNPT DPTDPTDPTD PTDPTDPTNP
TDLTEPEKPV NPEKPKPEKP KPEKPKPEKP KPSQPKPSTP KPSTPAPTPA PAPSAPNYNY
VAPVYSGANY TAQDAVTTYK QASTDGDLKF NKTNIAVPPL TKINTTTAED FIKSIAPRIS
QLAGQNNLYA SLIIAQAILE SGYGHSNVAA IYHNLFNIIG AFNGQSVTYR AYENFDQSLV
DYINLMLHGT TWNSKIYAGS WKVNSASVED AARSLQGIFA TDPEYAAKLI QIIKEYNLTQ
YDDIENLSEE FKNLDAPASP LLEAMPSDLK FPEYDGKQYP GASSYAWGNC TQYVYNRIFQ
LGGKIGQFMG NGGVWGSSGA AQGYYTTTIP QVGYAVSFPP GVAGASAEYG HVAFVEKVNK
DGSILVSEMN VKGLNVVNYR TISASDASLS TYIQPQK
//
