ID A0A0R1S9C4_9LACO Unreviewed; 273 AA.
AC A0A0R1S9C4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptidase M10 metallopeptidase domain-containing protein {ECO:0000259|Pfam:PF00413};
GN ORFNames=FC85_GL000087 {ECO:0000313|EMBL:KRL65537.1};
OS Lentilactobacillus diolivorans DSM 14421.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL65537.1, ECO:0000313|Proteomes:UP000052013};
RN [1] {ECO:0000313|EMBL:KRL65537.1, ECO:0000313|Proteomes:UP000052013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL65537.1,
RC ECO:0000313|Proteomes:UP000052013};
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 -!- 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:KRL65537.1}.
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; AZEY01000066; KRL65537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1S9C4; -.
DR PATRIC; fig|1423739.3.peg.93; -.
DR Proteomes; UP000052013; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR Pfam; PF00413; Peptidase_M10; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000052013};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..273
FT /note="Peptidase M10 metallopeptidase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038575649"
FT DOMAIN 106..234
FT /note="Peptidase M10 metallopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00413"
SQ SEQUENCE 273 AA; 29870 MW; B5839EA5ECDC6917 CRC64;
MKKNRLITAI VAAMLLAPAI PIAEAAAPSQ LSTITTAAAA KTKVASKARV VSAINRTADL
NPTGAVMTFN QPTYEAYGAL FDKQYNVGAM SSWKVFGKHN RAYVYTNSSA LQRYVTGAIK
NWNRALGQKT FVQGTKAHHT ITIQWQYNGA NLDWDGLYAN GKLKINKSLY DDPTYVPQSY
EAENKTTMPG ANDPNSAAYQ QQASKYWIAI TTHELGHSLG LDHSPYTSDI MYTDSETAGS
KGRIPVVSLS LQTPFHNVIS TEQNWRKTLG TGK
//
