ID K2PI96_9LACT Unreviewed; 405 AA.
AC K2PI96;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Serine protease, DegP/HtrA {ECO:0000313|EMBL:EKF51140.1};
GN ORFNames=C426_1493 {ECO:0000313|EMBL:EKF51140.1};
OS Lactococcus garvieae DCC43.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1231377 {ECO:0000313|EMBL:EKF51140.1, ECO:0000313|Proteomes:UP000006787};
RN [1] {ECO:0000313|EMBL:EKF51140.1, ECO:0000313|Proteomes:UP000006787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCC43 {ECO:0000313|EMBL:EKF51140.1,
RC ECO:0000313|Proteomes:UP000006787};
RX PubMed=23209230; DOI=10.1128/JB.01864-12;
RA Gabrielsen C., Brede D.A., Hernandez P.E., Nes I.F., Diep D.B.;
RT "Genome Sequence of the Bacteriocin-Producing Strain Lactococcus garvieae
RT DCC43.";
RL J. Bacteriol. 194:6976-6977(2012).
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:EKF51140.1}.
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DR EMBL; AMQS01000022; EKF51140.1; -; Genomic_DNA.
DR RefSeq; WP_003136051.1; NZ_AMQS01000022.1.
DR AlphaFoldDB; K2PI96; -.
DR MEROPS; S01.447; -.
DR PATRIC; fig|1231377.3.peg.1484; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000006787; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EKF51140.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003865438"
FT DOMAIN 284..383
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 405 AA; 41695 MW; 8CE2667BEABEC717 CRC64;
MAKKNIASLL ITGVAGGAIA LGGSAVYQSM TNTPTTTNSQ NNAVSTVNVQ VNTDTTKAIK
TISNTVVSVL NYQKSSSNED LDSIFGNGNR SNESSSSPQL AGEGSGVIYK KDGNTAYVVT
NYHVVEGASS LEVLMAGGQK VTAEVVGSDA FSDLAVLKID AKYVKETATF GNSDKLTVGE
PAIAVGSPLG SEYANSATEG IVSSLNRNVV LQNSQGQTIN VNAIQTDAAI NPGNSGGALI
NIEGQVIGIT SSKITSTPSG TSSSGVSVEG MGFAIPANDV VNIINKLEKD GKVIRPALGV
QMVNLSSLSQ NSLASLNLPE DVTNGVAVAE VQSGMPAAKA GLKQGDVIVK INDDEITSSV
NLQSTLYKSS IGDTIKVTYY RDGKKATANV KLDKTSSDIN FDKQN
//
