ID A0A0R1S9Z2_9LACO Unreviewed; 621 AA.
AC A0A0R1S9Z2;
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=Protease {ECO:0000313|EMBL:KRL63221.1};
GN ORFNames=FC85_GL001649 {ECO:0000313|EMBL:KRL63221.1};
OS Lentilactobacillus diolivorans DSM 14421.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL63221.1, ECO:0000313|Proteomes:UP000052013};
RN [1] {ECO:0000313|EMBL:KRL63221.1, ECO:0000313|Proteomes:UP000052013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL63221.1,
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KRL63221.1}.
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DR EMBL; AZEY01000104; KRL63221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1S9Z2; -.
DR STRING; 1423739.FC85_GL001649; -.
DR PATRIC; fig|1423739.3.peg.1729; -.
DR Proteomes; UP000052013; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000313|EMBL:KRL63221.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KRL63221.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052013}.
FT DOMAIN 195..621
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 621 AA; 69435 MW; E42305E1BECB4938 CRC64;
MVGGQTQAAS TSSSVSDVYK KLTTAKNLPP TPVKKRQTTY FDIILKSQNS NHIENDALAV
NTPGDTNFKH YLTPNQFGRK YGASPILISQ WVKLLKHHSL KAVPLKNRLI IRVFGKVNKI
DRLFQTNLNK AKYHQNPIQF GTKTPRIPKK LSRTVWTIIG LTDHNRDYIY PDTSLPFKRR
AKKRPSINSG FTSRFTKRYH VTPLYKQQLT GKGQTIGIIA FENVRKANIF RFWRHEKVAT
NPSRLQIKSV FSPPYCPSED IQNSDETTMD AEYAGSVAPD ANVKIYLSNT DSNLTNFIDV
YEQAFNDNVV SSTTNSYGLL DSGSIAILRH RHLLTPVYRQ VLSFVLAQGA IQGISNFTAS
GDSGALNYMV KSENGRELML DRTLNSSDFF DSNPFITSVG GTTLPFRVKT GYGIIINKHE
RAWGTDYLWP FFQKQFKLVQ KFPNSLFING MAGSTGGFSH QYQTPTYQLN VPGVNTFKAR
NLVSGLGQPV LGSNVVTGTD HGRNYPDVAA NADPATGYWI YRRTKKHPKN GWDLSGDGTS
IASPQYAATA ALINSQPGRK QMGFWNPQIY QLAQQPNSPF TPLNSTKDNS NLYYVGQPGT
VYNQATGLGI TNFDQLAKTY R
//
