ID A0A0U3NPC0_9LACT Unreviewed; 415 AA.
AC A0A0U3NPC0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine protease, DegP/HtrA {ECO:0000313|EMBL:ALV22377.1};
GN ORFNames=NY10_1779 {ECO:0000313|EMBL:ALV22377.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22377.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV22377.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV22377.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010796; ALV22377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3NPC0; -.
DR STRING; 1564681.NY10_1779; -.
DR KEGG; carc:NY10_1779; -.
DR PATRIC; fig|1564681.3.peg.1783; -.
DR Proteomes; UP000064734; 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; 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.
DR PROSITE; PS50106; PDZ; 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:ALV22377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064734};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 297..380
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 415 AA; 43524 MW; D69E95FE3B2D1344 CRC64;
MSQNNKKSTN ETKFKKRGSL KSGILGGVIG GLVVALLGGG YLYTMESDTP TNSTGIVDEN
GKVTTTDVSV NVTSEVTDAV AKVEDSVVSV VNMQEQNTEG FGGIFGSDSD GTNMSEDSSL
QTAGEGSGVI YKIDGDTAYV VTNNHVINES DAVEVLMKDG TKVEAEIIGT DIWTDLAVLS
IPSENVTKAA TFGDSDSLTV GEPAIAIGSP LGTNFASSVT QGIISAKNRS VDTDINGDGV
IDWEMTALQT DAAINPGNSG GALINIAGQV IGINSMKIST DTVEGMGFAI PSNDVVSIIN
QLETEGKVVR PVLGISLLDI SQISEQQQAS VLKLPKDVTA GVVVGQVQPD SAAEKGGLEQ
YDVIVKFNGE DVVDTISLRK EIYKTELGKE IEVEYYRNGK LEKTTITMTD TESIT
//
