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Database: UniProt
Entry: A0A0M4CW07_SPHS1
LinkDB: A0A0M4CW07_SPHS1
Original site: A0A0M4CW07_SPHS1 
ID   A0A0M4CW07_SPHS1        Unreviewed;       260 AA.
AC   A0A0M4CW07;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 11.
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=LH20_03180 {ECO:0000313|EMBL:ALC10947.1};
OS   Sphingopyxis sp. (strain 113P3).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC10947.1, ECO:0000313|Proteomes:UP000061305};
RN   [1] {ECO:0000313|EMBL:ALC10947.1, ECO:0000313|Proteomes:UP000061305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113P3 {ECO:0000313|EMBL:ALC10947.1,
RC   ECO:0000313|Proteomes:UP000061305};
RX   PubMed=26472829;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A.,
RA   Yamazoe A., Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain
RT   Sphingopyxis sp. 113P3 (NBRC 111507).";
RL   Genome Announc. 3:e01169-15(2015).
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; CP009452; ALC10947.1; -; Genomic_DNA.
DR   RefSeq; WP_053552961.1; NZ_CP009452.1.
DR   EnsemblBacteria; ALC10947; ALC10947; LH20_03180.
DR   KEGG; sphp:LH20_03180; -.
DR   PATRIC; fig|292913.6.peg.642; -.
DR   KO; K02654; -.
DR   OrthoDB; 2046608at2; -.
DR   Proteomes; UP000061305; 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:UP000061305};
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:UP000061305};
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     14     35       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     91    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    132    150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    174       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    194    220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    254       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       19     98       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      111    218       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   260 AA;  27788 MW;  9EB57BF6F316FB09 CRC64;
     MDAAAGCLPW GAEIALAALI GGVLGSFIAT LVLRWPAGRS LAGRSQCDGC NARLEARDLV
     PLFSALWLRG RCRLCGAPID KLHGRVELAS AFLATLALAL MPGAQGWIWA LFGWLLLPLA
     LLDARHMWLP DPLNALLALV GLIFAGPLMG TTLLERWLGA LAGGLTLALI AWSWRRAHGR
     EAMGGGDPKL VAAIGTWLGW QALPLLLLLA SLTGIGWALF SRGKGDRPLT LRRVPFGVFL
     CAAAFVVVPL WPWWTGLIAR
//
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