(data stored in ACNUC7421 zone)

SWISSPROT: Q3IID0_PSEHT

ID   Q3IID0_PSEHT            Unreviewed;       291 AA.
AC   Q3IID0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 73.
DE   RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU003794};
DE            EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794};
GN   Name=pilD {ECO:0000313|EMBL:CAI85478.1};
GN   OrderedLocusNames=PSHAa0380 {ECO:0000313|EMBL:CAI85478.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85478.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85478.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates
CC       the N-terminal (generally Phe) residue.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY: Typically cleaves a -Gly-|-Phe- bond to
CC       release an N-terminal, basic peptide of 5-8 residues from type IV
CC       prepilin, and then N-methylates the new N-terminal amino group,
CC       the methyl donor being S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; CR954246; CAI85478.1; -; Genomic_DNA.
DR   STRING; 326442.PSHAa0380; -.
DR   MEROPS; A24.001; -.
DR   EnsemblBacteria; CAI85478; CAI85478; PSHAa0380.
DR   KEGG; pha:PSHAa0380; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248584; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; POG091H01KW; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010627; Pept_A24A_N.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   Pfam; PF06750; DiS_P_DiS; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
DR   PRODOM; Q3IID0.
DR   SWISS-2DPAGE; Q3IID0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:CAI85478.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     28       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    134    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    161    179       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    206       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    218    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    261    278       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       15    127       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      140    247       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   291 AA;  31948 MW;  A5DAB18B637FBEBE CRC64;
     MQSQLWFYLT TIGLVSLCVG SFLNVVIYRL PLMMQHEWQG ECRLLLESEL KGNKADESES
     LNSTFNLVKP NSTCPKCKTA IKAWQNIPVV SWLFLKGKCA SCSNPISARY PIVEAITALL
     SLVVAYKLGA TEQALLYIAI TWALVALTFI DIDHMLLPDQ ITLPLVWLAL IAAVLGYTVT
     PTDAIIGAAC GYLSLWSVFW LFKLLTGKEG MGYGDFKLLA VFGALLGWQS LLTIILLSSV
     VGAIIGIALL TIQGKDKATP IPFGPYLAIA GWITMLWGEQ LQTSYFNLIG Y
//

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