ID A0A0R2AT73_9LACO Unreviewed; 421 AA.
AC A0A0R2AT73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:KRM69554.1};
GN ORFNames=FD06_GL001042 {ECO:0000313|EMBL:KRM69554.1};
OS Apilactobacillus ozensis DSM 23829 = JCM 17196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM69554.1, ECO:0000313|Proteomes:UP000052012};
RN [1] {ECO:0000313|EMBL:KRM69554.1, ECO:0000313|Proteomes:UP000052012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM69554.1,
RC ECO:0000313|Proteomes:UP000052012};
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 -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KRM69554.1}.
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DR EMBL; AYYQ01000003; KRM69554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2AT73; -.
DR STRING; 1423781.FD06_GL001042; -.
DR PATRIC; fig|1423781.4.peg.1082; -.
DR Proteomes; UP000052012; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRM69554.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052012};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 313..401
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 421 AA; 43790 MW; AAF00A24CA8737B1 CRC64;
MGALLMKKEN SYIWKASVAA LVAGLLGGGI AYGGINAFQN SGINTAVPTS SNSGGTATQS
NINVNVQNQT EKAYQAVKNS VVSVVNLKAA SQSDNQLAQM FGFESGNSSN SGKSKSELEA
SSEGSGLIYK KSGDSAYIVT NNHVVAGSSA LEVILSDGKK VEAKIVGRDE VTDLAVLKIN
SSVVNQVATF GNSDNIKVGE TSLAIGSPMG SSYASSLTQG IISAKKREVQ QTSSNGQATG
NTATVIQTDT AINPGNSGGP LINLAGQVIG INSMKLSSDG EGTSVEGIGF AIPSNEVVNI
INQLVEHGKV IRPALGIQYV DLTNISAQQQ KSILKLPESV KNGVVVMKTT SDSPAANAGI
SKYDVITKFA GKNIESQNDI RDILYKQKVG STVSVTYYHN GKAVTKDMKL DKQLSQINFG
K
//
