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Database: UniProt
Entry: C1AAY7_GEMAT
LinkDB: C1AAY7_GEMAT
Original site: C1AAY7_GEMAT 
ID   C1AAY7_GEMAT            Unreviewed;       296 AA.
AC   C1AAY7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 48.
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:BAH39393.1};
GN   OrderedLocusNames=GAU_2351 {ECO:0000313|EMBL:BAH39393.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH39393.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y.,
RA   Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S.,
RA   Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that
RT   represents a novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-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; AP009153; BAH39393.1; -; Genomic_DNA.
DR   STRING; 379066.GAU_2351; -.
DR   EnsemblBacteria; BAH39393; BAH39393; GAU_2351.
DR   KEGG; gau:GAU_2351; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248583; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   BioCyc; GAUR379066:G1G2N-2419-MONOMER; -.
DR   Proteomes; UP000002209; 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:UP000002209};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:BAH39393.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:BAH39393.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002209};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:BAH39393.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     25     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     90    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    116    137       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    149    167       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    173    197       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    226    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    269    290       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       33    115       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      127    241       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   296 AA;  31781 MW;  1FBD22EF9457EB1E CRC64;
     MAADFEFNGP LTAGLLHALP VLDQILVLLP FFVLGAAIGS FLNVCISRWP HELSVIKPRS
     RCPRCERPIA WHENIPLVSW LMLRGKCRGC ALPISVQYPL VELLVALGWV VSVYAYGVTL
     EALRVALFGT VLLGIAITDA KHYLIPDGFT ITGLVLVLVL AIVNLFVQDT SHFVSAWPAI
     LGACVGAGAI TLIGWIAEVI MKREAMGFGD TTLMAVVGAA VGAERALLTI IAGAFVGAVV
     FLLIVGPIVK VRTARRGEPF AFPDVPFGVF LAPAAMLVLL WGEALITWYV QRAFPA
//
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