ID F6FQ35_ISOV2 Unreviewed; 390 AA.
AC F6FQ35;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Peptidase S1 and S6 chymotrypsin/Hap {ECO:0000313|EMBL:AEG44841.1};
GN OrderedLocusNames=Isova_2112 {ECO:0000313|EMBL:AEG44841.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG44841.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) 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; CP002810; AEG44841.1; -; Genomic_DNA.
DR AlphaFoldDB; F6FQ35; -.
DR STRING; 743718.Isova_2112; -.
DR MEROPS; S01.513; -.
DR KEGG; iva:Isova_2112; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_043139_0_0_11; -.
DR Proteomes; UP000009236; 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: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:UP000009236};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 390 AA; 39011 MW; CC6D1C339992598A CRC64;
MTPVDLLLVV ALVAALVAGL GRGLLATVGG LAGLVAGGLA AFWVVPVVND ALPTSQWRAP
ATLAIAVMLP LLGASAGAGV GHGLRRQVDR TPLRPLERLL GGVANLLVAA VAISFVGTAV
KATGAPGLAQ AVSSSVVLRT IDDLTPTPVS RTLAQMRSAV LDDGLPRLDG LLGPRVAPAA
PDVDLADPAL EASARSVARI WGTAYACGTS STGSGFVVAP DRVVTNAHVV AGVERPLVEL
PGRAAREGRV VYFDPVADLA VVAVDALDAD PLPVAPTLAA GDTAAVQGYP YGGPFISTGA
QVLDVGTVRV PESGGIGGGD REVYSLAAEV HPGNSGGPVL TTDGEVVGVI FGRADSEEDL
AYAVTTAELL PVVAQATELD TAVEPGRCAA
//