ID K4RBJ6_STRDJ Unreviewed; 394 AA.
AC K4RBJ6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:CCK30620.1};
GN ORFNames=BN159_6241 {ECO:0000313|EMBL:CCK30620.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK30620.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK30620.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HE971709; CCK30620.1; -; Genomic_DNA.
DR RefSeq; WP_015660956.1; NC_020504.1.
DR AlphaFoldDB; K4RBJ6; -.
DR STRING; 1214101.BN159_6241; -.
DR MEROPS; S01.513; -.
DR KEGG; sdv:BN159_6241; -.
DR PATRIC; fig|1214101.3.peg.6324; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_043139_0_0_11; -.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000008043; 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:CCK30620.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:CCK30620.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
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..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 394 AA; 40809 MW; B6138721B3116CD7 CRC64;
MDLLDILLLL VILAYAASGY RRGLVAGCVS FAGFVGGAVI GVWVLPWLMD LVEPGTTAAT
VTAVLTVLVP AAVGHELAGR LALRLRRELD QGPLRVADGV GGAVANSVAV LIVAWVAASV
LAASSSPLLT SAIRDSRVLG TVQDAMPDTT PAWFSRATSA LTEAGFPQVF NPFENESTAE
VAKPTGDSVT AAATNAAKLS TVKIEGVSGT QGREGSGFVY APRHVMTNAH VVAGLDEPSV
RVGGVGPAYE SRVVLFDPDK DVAVLYVPEL SAPVLKWDDS AERGDSAVVA GYPEDGDLNL
QAATVASRVR ANGQNIYNDD IVTREIYSIR STVRPGNSGG PLLTTEGRVY GVVFARSTSD
AETGYVLTAA EVTEDAERAA DATAPVDTGE LVTS
//
