ID A0A0R2F9N6_9LACO Unreviewed; 222 AA.
AC A0A0R2F9N6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN ORFNames=FD14_GL000467 {ECO:0000313|EMBL:KRN24995.1};
OS Secundilactobacillus similis DSM 23365 = JCM 2765.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN24995.1, ECO:0000313|Proteomes:UP000051442};
RN [1] {ECO:0000313|EMBL:KRN24995.1, ECO:0000313|Proteomes:UP000051442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN24995.1,
RC ECO:0000313|Proteomes:UP000051442};
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:KRN24995.1}.
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DR EMBL; AYZM01000079; KRN24995.1; -; Genomic_DNA.
DR RefSeq; WP_057151857.1; NZ_AYZM01000079.1.
DR AlphaFoldDB; A0A0R2F9N6; -.
DR STRING; 1423804.FD14_GL000467; -.
DR PATRIC; fig|1423804.4.peg.505; -.
DR OrthoDB; 2148705at2; -.
DR Proteomes; UP000051442; 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; IPR021190; Pept_M10A.
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 PRINTS; PR00138; MATRIXIN.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 69..222
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
SQ SEQUENCE 222 AA; 25193 MW; C0D055373E97315F CRC64;
MNLLKQGLLL LGMLGGLVTE PLSSRAKLVT RTEFARGQLP RMTQWSQFQS ADRTTDRAPL
AVGPVWTPAT QRWQQTTITY RLAPMSAYYR QIWRSAARHW SRVSLINLVE TKAKSADITV
QTKKQPAHVA PSIVGMTTSR HYSRTKLANL NVLATATATL YRDTTKALRY TRLQRIHVAE
HEFGHTLGLQ HAPFQQSVMY YVTRDRTITV ADIRGIQRAY AN
//
