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Database: UniProt
Entry: M1YZF7_9FIRM
LinkDB: M1YZF7_9FIRM
Original site: M1YZF7_9FIRM 
ID   M1YZF7_9FIRM            Unreviewed;       254 AA.
AC   M1YZF7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   16-JAN-2019, entry version 21.
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   ORFNames=CUESP1_1824 {ECO:0000313|EMBL:SHD77187.1}, CULT_340020
GN   {ECO:0000313|EMBL:CCQ95975.1};
OS   [Clostridium] ultunense Esp.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Tissierellaceae.
OX   NCBI_TaxID=1288971 {ECO:0000313|EMBL:CCQ95975.1, ECO:0000313|Proteomes:UP000011752};
RN   [1] {ECO:0000313|EMBL:CCQ95975.1, ECO:0000313|Proteomes:UP000011752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Esp {ECO:0000313|EMBL:CCQ95975.1,
RC   ECO:0000313|Proteomes:UP000011752};
RX   PubMed=23538905; DOI=10.1128/genomeA.00107-13;
RA   Manzoor S., Muller B., Niazi A., Bongcam-Rudloff E., Schnurer A.;
RT   "Draft Genome Sequence of Clostridium ultunense Strain Esp, a
RT   Syntrophic Acetate-Oxidizing Bacterium.";
RL   Genome Announc. 1:e0010713-e0010713(2013).
RN   [2] {ECO:0000313|EMBL:SHD77187.1, ECO:0000313|Proteomes:UP000245423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77187.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; CARA01000210; CCQ95975.1; -; Genomic_DNA.
DR   EMBL; LT669839; SHD77187.1; -; Genomic_DNA.
DR   RefSeq; WP_005586058.1; NZ_LT669839.1.
DR   MEROPS; A24.019; -.
DR   EnsemblBacteria; CCQ95975; CCQ95975; CULT_340020.
DR   Proteomes; UP000011752; Unassembled WGS sequence.
DR   Proteomes; UP000245423; Chromosome chri.
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:UP000011752,
KW   ECO:0000313|Proteomes:UP000245423};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:CCQ95975.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:CCQ95975.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011752};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:CCQ95975.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    118    137       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    149    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    180    213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    225    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        7     90       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      101    208       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   254 AA;  28714 MW;  D20F5A4AA1264A1F CRC64;
     MTILIFLLGT IIGSFLNVCI HRIPKEESII FPGSYCPSCS TPLEWYDLVP VLSFLFLKGK
     CRYCGERISP RCPIVELLNG FIFVMLYSKF RFNLDFIFYT FLFSLFIIIT FIDLDYQIIP
     STMILFILVG SIVYKILNLM LYSIPVNFVN SLMGLGVSIL IFLIIFVVSK GGMGGGDVKL
     IGVLGFILGI SKIFLNIFLS FLAGGIISVL LLVFKIKGKK DPIPFGPFII LGFIITLFWG
     DKIINWYLVS FLLR
//
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