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Database: UniProt
Entry: A1AMP0_PELPD
LinkDB: A1AMP0_PELPD
Original site: A1AMP0_PELPD 
ID   A1AMP0_PELPD            Unreviewed;       261 AA.
AC   A1AMP0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 68.
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   OrderedLocusNames=Ppro_0982 {ECO:0000313|EMBL:ABK98610.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98610.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABK98610.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-
CC         terminal, basic peptide of 5-8 residues from type IV prepilin,
CC         and then N-methylates the new N-terminal amino group, the methyl
CC         donor being S-adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={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; CP000482; ABK98610.1; -; Genomic_DNA.
DR   RefSeq; WP_011734917.1; NC_008609.1.
DR   STRING; 338966.Ppro_0982; -.
DR   MEROPS; A24.019; -.
DR   EnsemblBacteria; ABK98610; ABK98610; Ppro_0982.
DR   KEGG; ppd:Ppro_0982; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248583; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; PPRO338966:GHL0-981-MONOMER; -.
DR   Proteomes; UP000006732; Chromosome.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006732};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ABK98610.1}; 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:UP000006732};
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     26       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    129    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    153    173       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    193    220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    227    245       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       13     96       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      107    215       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   261 AA;  28521 MW;  BF08C90B69FF9177 CRC64;
     MTPQLLFSVF SFILGAVVGS FLNVCICRMP RDESVVSPPS HCPGCGYRIR WYDNIPLVSY
     LLLRGRCRGC REKISPRYPL VELLNALLSL ALFLRFGPTL AFAVLFLFCS ALVVITFIDL
     EHQIIPDEIS LPGIVLGFIF SFFLRGHGWL NSLLGILLGG GSLLLVAYGY QLVTGKEGMG
     GGDIKLLAMM GAFLGWKSIP FIIFVSSLAG SVIGVSLMLI QKKDSKLAIP FGPYLALGAL
     LYVFYGPRLI SWYLTLGGLQ G
//
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