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Database: UniProt
Entry: A0A0S9BT28_9MICC
LinkDB: A0A0S9BT28_9MICC
Original site: A0A0S9BT28_9MICC 
ID   A0A0S9BT28_9MICC        Unreviewed;       394 AA.
AC   A0A0S9BT28;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Colicin V production protein {ECO:0000313|EMBL:KQN84530.1};
GN   ORFNames=ASE96_17270 {ECO:0000313|EMBL:KQN84530.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN84530.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN84530.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN84530.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN84530.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN84530.1,
RC   ECO:0000313|Proteomes:UP000051467};
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:KQN84530.1}.
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DR   EMBL; LMLR01000016; KQN84530.1; -; Genomic_DNA.
DR   RefSeq; WP_056433751.1; NZ_LMLR01000016.1.
DR   AlphaFoldDB; A0A0S9BT28; -.
DR   STRING; 1736232.ASE96_17270; -.
DR   OrthoDB; 9766361at2; -.
DR   Proteomes; UP000051467; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   394 AA;  39906 MW;  28551028ED202891 CRC64;
     MFGLTILDLV LILTLLSYLF HGLRNGFLVT VGGIAGFAAG AVAAFVSVPI VSGLVEDSGW
     RLTAIIATAV LLMMLGHGIG TAIGRNIRSV VKINPLRSVD RLAGGGVNVV VSALVMSMLA
     FSIGALGVPF VSQPLAESKV IRFIDGVTPV PLKTSMAQLR SAVIGEGIPT LFEGIGEGQP
     VAIPDTSTDT PALNRAADSV LKIAGTAYQC GQNQTGTGFV VSPGRVVTNA HVVAGVPEPV
     VEIPGAGALP GRVVYFDTQH DLAVVAVDGL RTAPLPLSSD LAAGSPAAFA GYPHGGPFQS
     KPATVQDIAT VLVPDIYGNN PAPADVYRIA GDVQPGNSGG PLLTNDGQVA GVIFAKATSG
     SPLGYAITMA DLRPVASQAP GLANAVSPGQ CIQK
//
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