GenomeNet

Database: UniProt
Entry: A0A0P0SJH6_9PSEU
LinkDB: A0A0P0SJH6_9PSEU
Original site: A0A0P0SJH6_9PSEU 
ID   A0A0P0SJH6_9PSEU        Unreviewed;       399 AA.
AC   A0A0P0SJH6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:ALL84640.1};
GN   ORFNames=AD017_14255 {ECO:0000313|EMBL:ALL84640.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84640.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL84640.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84640.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CP012184; ALL84640.1; -; Genomic_DNA.
DR   RefSeq; WP_060576396.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SJH6; -.
DR   STRING; 1096856.AD017_14255; -.
DR   KEGG; pecq:AD017_14255; -.
DR   PATRIC; fig|1096856.3.peg.2991; -.
DR   OrthoDB; 9766361at2; -.
DR   Proteomes; UP000066228; Chromosome.
DR   GO; GO:0016020; C: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   GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR003825; Colicin-V_CvpA.
DR   InterPro; IPR047680; MarP-like.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; NF033740; MarP_fam_protase; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR   Pfam; PF02674; Colicin_V; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ALL84640.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:ALL84640.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   399 AA;  41513 MW;  16EC48C2767E469C CRC64;
     MSWVDVVVVV LALLAAASGW RHGVAVALLS FLGVLTGAVL GLRLAPLLAA QVESQQAKVL
     LGIGAVVLLV ALGEATGVYL GRFIRDRIRG EGTLKVDSTL GAGVQAVAVV VAAWLIALPL
     ASTSFATLTS GLRDSRVLGA VDGVMPDAAR QLPSELRQIL DDSGFPDVVS PFSRTPVAAV
     GPPDANLVQN PVVTEVRDRV LKVRGRAPSC RRALEGTGFV VAPQRVMTNA HVVAGTSSTT
     VEVTTASGRT RQLDAEVVFY DPQVDVAVMD VPALEEEPLQ FSPDPARVGD DVVILGYPLD
     GPYTVTPGKV RERIRLRGPD IYEQGSVVRD VYTVRAVVRS GNSGGPMIAP DGRVVGVVFG
     AALDDSETGF VLTAEQAAQA LNVAANESAS PVDTGECAS
//
DBGET integrated database retrieval system