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Database: UniProt
Entry: A0A1Q4D4Y1_9PSEU
LinkDB: A0A1Q4D4Y1_9PSEU
Original site: A0A1Q4D4Y1_9PSEU 
ID   A0A1Q4D4Y1_9PSEU        Unreviewed;       222 AA.
AC   A0A1Q4D4Y1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Prepilin type IV endopeptidase peptidase domain-containing protein {ECO:0000259|Pfam:PF01478};
GN   ORFNames=BGP03_02240 {ECO:0000313|EMBL:OJY39200.1};
OS   Pseudonocardia sp. 73-21.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY39200.1, ECO:0000313|Proteomes:UP000186163};
RN   [1] {ECO:0000313|EMBL:OJY39200.1, ECO:0000313|Proteomes:UP000186163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-21 {ECO:0000313|EMBL:OJY39200.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801}.
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:OJY39200.1}.
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DR   EMBL; MKVV01000098; OJY39200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4D4Y1; -.
DR   STRING; 1895809.BGP03_02240; -.
DR   Proteomes; UP000186163; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.1220; -; 1.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE_N-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..181
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   222 AA;  21375 MW;  E5EE307E735C9E4C CRC64;
     MALSVLPVVP PPVAGALLFA VAGCGAGTAA RVVLGRMRRG ARVRAPVCEL ALAVLWAAVG
     AGWIGGLVPG RWLPVLLGAS WLAVAGSVVD VLHHRLPDAL TAPAWPAALL VVLPLGPGAL
     GRAAVGAVVA AAVHAAVHRA APRALGGGDV KLAGPLGAVL AAAAWPALAL AGLLAAVLSA
     LVAAVLLVAG RTGRAGAVPH GPSMLVATWL VLAGAAFGAG AG
//
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