ID A0A139NEJ1_9STRE Unreviewed; 381 AA.
AC A0A139NEJ1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine protease, DegP/HtrA, do-like protein {ECO:0000313|EMBL:KXT74227.1};
GN ORFNames=STRDD10_01098 {ECO:0000313|EMBL:KXT74227.1};
OS Streptococcus sp. DD10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT74227.1, ECO:0000313|Proteomes:UP000072050};
RN [1] {ECO:0000313|EMBL:KXT74227.1, ECO:0000313|Proteomes:UP000072050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD10 {ECO:0000313|EMBL:KXT74227.1,
RC ECO:0000313|Proteomes:UP000072050};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXT74227.1}.
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DR EMBL; LQRE01000086; KXT74227.1; -; Genomic_DNA.
DR RefSeq; WP_067193732.1; NZ_KQ969159.1.
DR AlphaFoldDB; A0A139NEJ1; -.
DR STRING; 1777878.STRDD10_01098; -.
DR PATRIC; fig|1777878.3.peg.1210; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000072050; 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:KXT74227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000072050};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..362
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 381 AA; 40034 MW; 09C6EECECE796DE1 CRC64;
MKKYVQPLFV LIIGFIGGLL GALLLTQQQD SSVISGQNNT KTVSYSNSNS TTEAVKKVQD
AVVSVINYSQ TEGSSSSLDN EESISGEGSG VIYKKDKQYA YIATNNHVVD GAQSLDIQLS
DGTKVAGELV GADTYSDLAV VRIPADKAPA VAEFADSSKV NVGETAIAIG SPLGTEYANS
VTQGIVSSLS RNVSLTTEDG RAVSTNAIQT DAAINPGNSG GPLINIQGQV IGITSSKISV
SRSSGVAVEG MGFAIPSNDV VNIISQLEEN GSVSRPALGI QMINLANLSS SDISRLNIPS
TLKGGVVVRS VQENMPADGK LKQYDVITKV DDTEILSTSD LQSALYKHQL NDEINITFYR
NGKEESTTIK LTKSSQDLST E
//
