ID A0A0R2LFJ1_9LACO Unreviewed; 187 AA.
AC A0A0R2LFJ1;
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=Zn-dependent protease {ECO:0000313|EMBL:KRO00263.1};
GN ORFNames=IV54_GL000586 {ECO:0000313|EMBL:KRO00263.1};
OS Levilactobacillus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=616990 {ECO:0000313|EMBL:KRO00263.1, ECO:0000313|Proteomes:UP000051906};
RN [1] {ECO:0000313|EMBL:KRO00263.1, ECO:0000313|Proteomes:UP000051906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22467 {ECO:0000313|EMBL:KRO00263.1,
RC ECO:0000313|Proteomes:UP000051906};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KRO00263.1}.
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DR EMBL; JQCA01000126; KRO00263.1; -; Genomic_DNA.
DR RefSeq; WP_057879084.1; NZ_JQCA01000126.1.
DR AlphaFoldDB; A0A0R2LFJ1; -.
DR STRING; 616990.IV54_GL000586; -.
DR PATRIC; fig|616990.3.peg.629; -.
DR OrthoDB; 2148705at2; -.
DR Proteomes; UP000051906; 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:UniProtKB-KW.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRO00263.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..187
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006419931"
FT DOMAIN 32..187
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 187 AA; 20773 MW; 850D03FB8064723B CRC64;
MLKKIVKWTV LVIATIVLTL TSFTSTILAA SKTPSWGHWD DTTITYKTAS TSSYYKSVWK
NAVKRWNKVG VVQLRAAKSG EKADITLTSS KSLSTKSGKL AGYTNYSYLK KSDNENEIVS
AKSTLNRSLL SKYKYSKNQR TNVATHEIGH AIGLSHSKSE DSVMYASDRY ASIDHQDKVG
LQSAYED
//
