ID   I4MXI2_9PSED            Unreviewed;       102 AA.
AC   I4MXI2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Prolipoprotein signal peptidase (Signal peptidase II.) {ECO:0000313|EMBL:EIK93922.1};
GN   ORFNames=PMM47T1_24348 {ECO:0000313|EMBL:EIK93922.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK93922.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK93922.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK93922.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|RuleBase:RU004181}.
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:EIK93922.1}.
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DR   EMBL; AJWX01000030; EIK93922.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4MXI2; -.
DR   STRING; 1179778.PMM47T1_24348; -.
DR   PATRIC; fig|1179778.3.peg.4837; -.
DR   Proteomes; UP000004339; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000313|EMBL:EIK93922.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   102 AA;  10948 MW;  ABC568B3C51B159D CRC64;
     MPPLVKQLIF ILAVAVVVWA GYWALRHWAA LPHKAFALYA IALGDVGNLI DRVFRDGHVV
     GYLIVNVGAL HTGVFNIADI AITAGAMVLA WDLFAKADGK PA
//