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Database: UniProt
Entry: A3DDQ7_CLOTH
LinkDB: A3DDQ7_CLOTH
Original site: A3DDQ7_CLOTH 
ID   A3DDQ7_CLOTH            Unreviewed;       281 AA.
AC   A3DDQ7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=Cthe_0852 {ECO:0000313|EMBL:ABN52086.1};
OS   Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 /
OS   NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium
OS   thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Hungateiclostridiaceae; Hungateiclostridium.
OX   NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN52086.1, ECO:0000313|Proteomes:UP000002145};
RN   [1] {ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
RC   / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
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., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABN52086.1, ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536
RC   / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RX   PubMed=24295562; DOI=10.1186/1754-6834-6-179;
RA   Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M.,
RA   Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H.,
RA   Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.;
RT   "Global transcriptome analysis of Clostridium thermocellum ATCC 27405
RT   during growth on dilute acid pretreated Populus and switchgrass.";
RL   Biotechnol. Biofuels 6:179-179(2013).
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; CP000568; ABN52086.1; -; Genomic_DNA.
DR   RefSeq; WP_011837918.1; NC_009012.1.
DR   STRING; 203119.Cthe_0852; -.
DR   MEROPS; A24.019; -.
DR   EnsemblBacteria; ABN52086; ABN52086; Cthe_0852.
DR   GeneID; 35804531; -.
DR   KEGG; cth:Cthe_0852; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248583; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; CTHE203119:G1G86-887-MONOMER; -.
DR   Proteomes; UP000002145; 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:UP000002145};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ABN52086.1}; 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:UP000002145};
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     15     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     75       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     87    105       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    112    130       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    158       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    170    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    214    241       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    248    268       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       25    108       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      119    234       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   281 AA;  31609 MW;  8B9CCC1E8413BE4E CRC64;
     MGTSLNLGLL FETGFTVFCY ISVALLGLLV GSFLNVCIYR IPNDESVVRP RSHCMKCGHT
     LGALDLVPVF SYLFLKGRCR YCGEKISPRY ALVELLTSVV YLLLFWKYGL SVDFLASAYL
     MSVLIAVFFI DLDHMIIPNK LVVAALVGGV LPFVYNIFRP MDIYVDRKWW NPLLGAFIGF
     GFLLLVAIVG YLVYKTDEAM GGGDVKLFAP IGLFLGWKMT IVALFISFVS AGIVSIVLLL
     LKKKERRSTF VFGPFIVMGT FFTYLFGWEL LEWYLSTLLH V
//
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