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Database: UniProt
Entry: A0A1E5P6S5_9ACTN
LinkDB: A0A1E5P6S5_9ACTN
Original site: A0A1E5P6S5_9ACTN 
ID   A0A1E5P6S5_9ACTN        Unreviewed;       274 AA.
AC   A0A1E5P6S5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:OEJ25243.1};
GN   ORFNames=AS594_12820 {ECO:0000313|EMBL:OEJ25243.1};
OS   Streptomyces agglomeratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ25243.1, ECO:0000313|Proteomes:UP000095759};
RN   [1] {ECO:0000313|EMBL:OEJ25243.1, ECO:0000313|Proteomes:UP000095759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ25243.1,
RC   ECO:0000313|Proteomes:UP000095759};
RA   Chen X.;
RT   "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT   novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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:OEJ25243.1}.
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DR   EMBL; MEHJ01000001; OEJ25243.1; -; Genomic_DNA.
DR   RefSeq; WP_069932962.1; NZ_MEHN01000001.1.
DR   AlphaFoldDB; A0A1E5P6S5; -.
DR   STRING; 285458.BGM19_23990; -.
DR   OrthoDB; 2087435at2; -.
DR   Proteomes; UP000095759; 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; IPR014032; Peptidase_A24A_bac.
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.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095759};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        96..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..235
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   274 AA;  27277 MW;  666F0C367FB9DCC9 CRC64;
     MYVTLIAAAA LWGALTGLLV PRAAYRLAVE PEEGWRAACP AGHPFTGPAR GWLGTARCAR
     CAAAVGAAAP VRTPDGAAED AGAPDLPSDG APYPRAVVPA VLTALACALL AAGTGGRPEL
     GVWLLLAPFG VLLAVVDLRV HRLPDVLTLP LAAAAALLLG LAALLPGDGG SWPGALLGGA
     ALGGGYFVLF LINPNGMGFG DVKLAVALGT ALGWYGWPVF FAGAFAGFLL GAVYGAGLVI
     LRRAGRRTAI PFGPFMITGT LAGLLLGGLA ASAA
//
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