ID A0A0R2LXF0_9LACO Unreviewed; 442 AA.
AC A0A0R2LXF0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:KRO04146.1};
GN ORFNames=IV54_GL001668 {ECO:0000313|EMBL:KRO04146.1};
OS Levilactobacillus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=616990 {ECO:0000313|EMBL:KRO04146.1, ECO:0000313|Proteomes:UP000051906};
RN [1] {ECO:0000313|EMBL:KRO04146.1, ECO:0000313|Proteomes:UP000051906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22467 {ECO:0000313|EMBL:KRO04146.1,
RC ECO:0000313|Proteomes:UP000051906};
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:KRO04146.1}.
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DR EMBL; JQCA01000043; KRO04146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2LXF0; -.
DR STRING; 616990.IV54_GL001668; -.
DR PATRIC; fig|616990.3.peg.1765; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000051906; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:KRO04146.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 328..416
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 45403 MW; CAA0E46F3C440F3F CRC64;
MDNNNQNNQS NDNNETTPTP QTRKRGGLTL TKVAVTALVA GLLGGGAAYG GITYFNNSGI
NDTAVPSGSN STGNTKTSNV TVNVSSQSTK AFNKVKGAMV SVVNLQKQNN NSTLGQLFGQ
ESSSSDSSSS KAALEEASEG SGVVYKKDGN TAYIVTNNHV VSGSSALRVV TSSGKQLQAK
LVGKDSVTDL AVLKVNGASL KTVASFGNSD DIKVGETALA IGSPLGSQYA TSLTEGIISA
KKRTIETTNS AGTQTGNATV IQTDAAINPG NSGGALINVG GQVVGITSSK IASDAEGTSV
EGMGFAIPSN EVVNIINQLV KKGKVVRPAL GITYVDLANV SSSQQKSVLK LPSSVDAGVV
VMSASADSPA KKAGLAKYDV ITELGGHEIS DQSTLRDLLY KYKLNDTVLL TYYHNGKKKT
TKVKLTETSS QLSKTTSATS ES
//