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Database: UniProt
Entry: A0A1B1MEX4_STRLN
LinkDB: A0A1B1MEX4_STRLN
Original site: A0A1B1MEX4_STRLN 
ID   A0A1B1MEX4_STRLN        Unreviewed;       259 AA.
AC   A0A1B1MEX4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Type IV peptidase {ECO:0000313|EMBL:ANS67156.1};
GN   ORFNames=SLINC_4932 {ECO:0000313|EMBL:ANS67156.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS67156.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS67156.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS67156.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT   actinobacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; CP016438; ANS67156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1MEX4; -.
DR   STRING; 1915.SLINC_4932; -.
DR   KEGG; sls:SLINC_4932; -.
DR   PATRIC; fig|1915.4.peg.5479; -.
DR   Proteomes; UP000092598; Chromosome.
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:UP000092598};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        84..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..223
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   259 AA;  26976 MW;  86B003FA0315B5EE CRC64;
     MLVVLAALWG AAAGALVPRA AYRFSVPPEE PWREHCPGGH PVRGWLGRAR CAECADARPA
     PDARPAPDTT AVVRRASGGY GPRTALVSFV TALLCAGIAA ATDTRPEVAV WLLLAPVGVL
     LTVVDLRVRR LPDILTLPSA AATLALLGLV SLVPEHTGHW SSAALGTLAL GAGYYLLWRI
     NPGGMGFGDV KLALLAGAVL GWYGWGTVLL GTLTGFVLGA LYGWTLVLLR RADRKTAIPF
     GPFLIAGVYA GLLIGAYAA
//
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