ID A0A0Q8VA47_9ACTN Unreviewed; 394 AA.
AC A0A0Q8VA47;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Peptidase S1 {ECO:0000313|EMBL:KRC54038.1};
GN ORFNames=ASE19_08175 {ECO:0000313|EMBL:KRC54038.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC54038.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC54038.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC54038.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC54038.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC54038.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRC54038.1}.
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DR EMBL; LMIP01000010; KRC54038.1; -; Genomic_DNA.
DR RefSeq; WP_056895470.1; NZ_LMIP01000010.1.
DR AlphaFoldDB; A0A0Q8VA47; -.
DR OrthoDB; 9766361at2; -.
DR Proteomes; UP000051414; 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:UP000051414};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 394 AA; 40778 MW; 5831FAA3EEE61116 CRC64;
MNVLDWLLVL LVLAYALSGY WQGFVTGAFA TVGLLAGGLA GIFLAPLLLS KLDPSLAVSL
GALFIVILCA SLGQALLQYA GARVRERITW QPARALDAVG GALLSALAVL LVAWALGVAI
SGTRIGSVTS MVRSSVVLGK VNDALPDAAP NVLQAFNNVV GTGFFPRYLE PFAPEQIVEV
QPGPSNLPRT AAVRAVRPSV VKIRGGNKCG RGVEGTGFVY APDRVMTNAH VVAGVQDPEV
SIGGGTELAR VVYYDRKLDI AVLALDTGDA PVLAFDQTTE AEDPIAIIGY PQDGPFDVQT
GRVRAMQNLR SPDIYGAGTV VREVFSLRGL VRPGNSGGPI VTPQGKVAGV VFAASVTDPE
TGYALTAKQV AETAERGAAA GSDGREADTG NCAA
//
