ID A0A0R2A9D9_9LACO Unreviewed; 430 AA.
AC A0A0R2A9D9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:KRM60683.1};
GN ORFNames=FC26_GL000159 {ECO:0000313|EMBL:KRM60683.1};
OS Paucilactobacillus vaccinostercus DSM 20634.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM60683.1, ECO:0000313|Proteomes:UP000051733};
RN [1] {ECO:0000313|EMBL:KRM60683.1, ECO:0000313|Proteomes:UP000051733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM60683.1,
RC ECO:0000313|Proteomes:UP000051733};
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:KRM60683.1}.
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DR EMBL; AYYY01000061; KRM60683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2A9D9; -.
DR STRING; 1423813.FC26_GL000159; -.
DR PATRIC; fig|1423813.3.peg.171; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000051733; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRM60683.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051733};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..407
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 51..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 44139 MW; 6CF0AD1FA108E2A2 CRC64;
MMDNQQKTPK KKRGFNLWWK VGVVALFAGL VGGGIAYGVG YLIDNGYATS SSTAVPKGSN
KSGGTKVNEN KVTGSTQSTK AFKSVKAAVV SVVNLQAQSS STGSLGIYGT TDSSSSSSSS
SSSSLEASSE GSGVIYKKDG NTAYIVTNNH VVSGSSALEV ILSNGKKLSA TIVGTDSTTD
LAVIKINSSD VTTIASFGNS NQIEAGQDVL AIGSPLGSEY ATSVTKGIIS AKKRTVQVQD
NSGNTTANAS VIQTDAAINP GNSGGPLVNM AGQVIGINSM KLSSDDDGTS VEGMGFSIPS
NEVVSVINQL VKNGKITRPA LGIELVSLDN VSAAQQKSIL KLPTSVNKGI VVMKILSPSS
AGNAGLQKYD VITEMDGTKI TSEATLKDVL YKHKVGDSVS VKYYRDGQLK SATIKLSEST
ALLSSDSSSE
//
