GenomeNet

Database: UniProt
Entry: A6T4T8_KLEP7
LinkDB: A6T4T8_KLEP7
Original site: A6T4T8_KLEP7 
ID   A6T4T8_KLEP7            Unreviewed;       266 AA.
AC   A6T4T8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   10-APR-2019, entry version 59.
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=pulQ {ECO:0000313|EMBL:ABR75609.1};
GN   ORFNames=KPN_00149 {ECO:0000313|EMBL:ABR75609.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR75609.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR75609.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR75609.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000647; ABR75609.1; -; Genomic_DNA.
DR   RefSeq; WP_004145898.1; NC_009648.1.
DR   MEROPS; A24.A10; -.
DR   EnsemblBacteria; ABR75609; ABR75609; KPN_00149.
DR   KEGG; kpn:KPN_00149; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248584; -.
DR   KO; K02464; -.
DR   OMA; VFWLFKL; -.
DR   BioCyc; KPNE272620:G1G8J-156-MONOMER; -.
DR   Proteomes; UP000000265; 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:UP000000265};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   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:UP000000265};
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     13     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    119    135       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    147    166       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    172    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    233       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    245    262       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    109       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      123    231       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   266 AA;  29389 MW;  E66D7E4D5416129E CRC64;
     MTTLAALSLH FPFVWYGFLL LFGLALGSFY NVVIYRLPRM LTQTADDERI TLSTPGSSCP
     QCRQPIAWRD NIPLLSFLWL GRRARCCQAP IAWSYPLTEL ATGLLFILAG ALLAPGLPLA
     GGLVLLSFLL ILARIDARTQ LLPDRLTLPL LWAGLLFNLN EVYIALPDAV AGAMAGYLAL
     WSVYWLFRLL TGKEALGYGD FKLLAALGAW CGWQVLPQVL LLASASGLVW TLLQRLWTRQ
     SLQQPLAFGP WLALAGGGIF LWQQMV
//
DBGET integrated database retrieval system