ID A0A0R1HL86_9LACO Unreviewed; 629 AA.
AC A0A0R1HL86;
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=Peptidase S53 propeptide {ECO:0000313|EMBL:KRK47502.1};
GN ORFNames=FC96_GL002428 {ECO:0000313|EMBL:KRK47502.1};
OS Secundilactobacillus kimchicus JCM 15530.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK47502.1, ECO:0000313|Proteomes:UP000050911};
RN [1] {ECO:0000313|EMBL:KRK47502.1, ECO:0000313|Proteomes:UP000050911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK47502.1,
RC ECO:0000313|Proteomes:UP000050911};
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:KRK47502.1}.
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DR EMBL; AZCX01000008; KRK47502.1; -; Genomic_DNA.
DR RefSeq; WP_056942847.1; NZ_AZCX01000008.1.
DR AlphaFoldDB; A0A0R1HL86; -.
DR STRING; 1302272.FC96_GL002428; -.
DR PATRIC; fig|1302272.5.peg.2474; -.
DR Proteomes; UP000050911; 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:InterPro.
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; 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.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050911};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038990945"
FT DOMAIN 191..629
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 629 AA; 68244 MW; 9EF4D43EE7196B60 CRC64;
MKMARKRLVA ALAGAAFVAG VQLTVAPQAA EAKVKAKSSQ YAVSVALKPT DQAGMVDQVY
ATADPTSDQY RKYLTPRDVA DKYGRSGSDI NQFKRYFKKY HVQANPYAGN LFLKVKGSYG
NVKRAFHAKL SKHRTVYKLP SALKRQVSSV IGLVGTRKAL LQAQGFKLKT KIDTSGQTPA
LTGQKSTFSE KYGPAKFADQ YQLDKVYERQ LTGKGQRIGL VAAADFYKSD VQKYLKQNGL
ATDVSRIHKI YLGSKKASQY TMSVDASMQA EVTLDVEQAA SVAPGADVDV YIYPEADKVM
SPDMSLLHTF NAAISDNLDK QLSTSIAMGN EVTGLGSDLS ETKQQYSAAY NQAFEQAALQ
GITVFNASGD SGPYSAVSAK FNQDMMTSPY EVSVGGTTLP FEKIENGHVV HVKKERAWGN
IYNINPLAKF LRQPYPAGGG GFSRLNATPR YQVGVPGVNT FTAIKHLQYK KKGVFKLSLF
GHRFKIPLPA YFKVIKNPQL IHGTGTGRNL PDIAGNADPD TGYGLCLTAA HSKKEKGQTV
WQIAGGTSAT APQMAAASAV MNSGLSQPAG FWNPQIYKYA QASDSPFTPL NDTFNNDNLY
YAGTPGTLYN QATGLGTVNF DQLYTKFKG
//
