ID I6T6A2_ENTHA Unreviewed; 428 AA.
AC I6T6A2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Serine protease DO {ECO:0000313|EMBL:AFM70226.1};
GN OrderedLocusNames=EHR_06435 {ECO:0000313|EMBL:AFM70226.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM70226.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM70226.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003504; AFM70226.1; -; Genomic_DNA.
DR RefSeq; WP_010737045.1; NZ_KB946228.1.
DR AlphaFoldDB; I6T6A2; -.
DR GeneID; 56786578; -.
DR KEGG; ehr:EHR_06435; -.
DR PATRIC; fig|768486.10.peg.521; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_2_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002895; Chromosome.
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.
DR PROSITE; PS50106; PDZ; 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:AFM70226.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002895};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..402
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 44582 MW; EA9CFB3F9D48FA88 CRC64;
MERKDVTPKM KKNNGIWRKL GLGLVGGIIG GLVTAGIFYA VMGSGNAASN SGGHQNSAGE
TVVENVKVNV DSDITNAVDK VQDAVVSVIN LQSQNQGTNG FGQLFGQQQQ ESSDDSNLEA
SSEGSGVIYK KSGNSAYIVT NNHVVEGQQG LEVLLKDGTK VKAELVGTDA YSDLAVLKIS
ADKVNKVASF GDSNSLKVGE PAIAIGSPLG SEYANSVTSG IISSLNRQVT STNESNQTVN
INAIQTDAAI NPGNSGGPLV NIEGQVIGIN SSKIASTSAS SSGVSVEGMG FAIPSNDVVN
IINQLEKDGK VTRPALGITM VDLSAVSTQQ QEQILKIPES VTNGVIVTSV QPATPAEKAG
LKQYDVITKI DDTDVSSGVE LQSVLYQKKV GDSVKVTYYR GKEKKTTTIQ LTIDQSALKQ
SQSENSGN
//
