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Database: UniProt
Entry: A0A285QML7_9ACTN
LinkDB: A0A285QML7_9ACTN
Original site: A0A285QML7_9ACTN 
ID   A0A285QML7_9ACTN        Unreviewed;       394 AA.
AC   A0A285QML7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Colicin V production protein {ECO:0000313|EMBL:SOB83200.1};
GN   ORFNames=SAMN06272789_3401 {ECO:0000313|EMBL:SOB83200.1};
OS   Streptomyces sp. 1331.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB83200.1, ECO:0000313|Proteomes:UP000219030};
RN   [1] {ECO:0000313|Proteomes:UP000219030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA   Varghese N., Submissions S.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; OBMJ01000001; SOB83200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285QML7; -.
DR   Proteomes; UP000219030; Unassembled WGS sequence.
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:InterPro.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219030};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   394 AA;  40984 MW;  FA5FEF0A2FF2BE97 CRC64;
     MNVLDVLLIL AAVGFAVSGY RQGFVVGVLS LVGFLGGGLL AVELLPLLLD HLSPGTTASV
     VAVVVVIVLA AVGQAITAHF GWKLRGHIDR RPARVLDASG GAVVNVVSML LVAWLIGSAL
     AGASLPTVSK QVRSSAILGG VQNALPSDAP NWFSDFSKVL ARNGFPQVFN PFEHEPITQV
     DTPDPALAAS PAVARARQSL VKVVGTATSC GKTLEGSGFV FAPHRVMTNA HVVGGVNEPT
     VQIGGVGQLY DATVVRYDWQ RDIAVLDVPK LNAPALTFAG EAKTNDSAIV AGFPENGAFN
     VQPARIRGRI QANGPDIYHR GQVMRDVYSV RSVVRQGNSG GPLLTPDGQV YGVVFAKSLD
     SADTGYVLTA AEVREDVQQG GAATARVDTQ GCAL
//
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