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Database: UniProt
Entry: A0A0R1QE31_9LACO
LinkDB: A0A0R1QE31_9LACO
Original site: A0A0R1QE31_9LACO 
ID   A0A0R1QE31_9LACO        Unreviewed;       474 AA.
AC   A0A0R1QE31;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:KRL39259.1};
GN   ORFNames=FD01_GL002627 {ECO:0000313|EMBL:KRL39259.1};
OS   Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL39259.1, ECO:0000313|Proteomes:UP000051790};
RN   [1] {ECO:0000313|EMBL:KRL39259.1, ECO:0000313|Proteomes:UP000051790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL39259.1,
RC   ECO:0000313|Proteomes:UP000051790};
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:KRL39259.1}.
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DR   EMBL; AZEU01000302; KRL39259.1; -; Genomic_DNA.
DR   RefSeq; WP_056965021.1; NZ_AZEU01000302.1.
DR   AlphaFoldDB; A0A0R1QE31; -.
DR   PATRIC; fig|1423769.4.peg.2836; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000051790; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRL39259.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051790};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          358..446
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  48125 MW;  E51BBA1101BD5F23 CRC64;
     MDNQSHNFQE QQPDQKPQKP HNGLKQTAIV AVVAAVIGGG VGGGAAYFGL KNAAESSLGV
     TSTSQKAGTT QVSNVSVKES SSSTTAAAKV KNAVVSVVNL QKAQSTSSGL DDWSDYFGSS
     DSNGSSSYGS DSSGSDTTSG ATTSGDSSRS SSSSSDSSDL EEYSEGSGVI YQKKDGKAYI
     VTNNHVVEDS DALEVILSDG TKVTAKKVGT DATTDLAVLS ISASKVTTVA SFGDSSALQA
     GQTVLAIGSP LGSQYASSVT QGIVSATSRT VDVTDEDTNQ TVGQETVIQT DAAINSGNSG
     GPLINLSGQV IGINSMKLSS SSSDSSTATI EGMGFAIPSN EVVSIINQLV ENGKVVRPAL
     GVEIRDLSSV TASQQSSVLK LPTSVTGGAV IAGFTSGSIA KSAGLSKYDV IVGIDSDKVT
     GVADLRTALY KHNVNDTVKI TYYHQGTKKT TNVKLTETTD SLSSSDSSST SSSN
//
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