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Database: UniProt
Entry: A0A0R2T3R9_9GAMM
LinkDB: A0A0R2T3R9_9GAMM
Original site: A0A0R2T3R9_9GAMM 
ID   A0A0R2T3R9_9GAMM        Unreviewed;       284 AA.
AC   A0A0R2T3R9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-MAY-2019, entry version 8.
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=ABR85_05505 {ECO:0000313|EMBL:KRO81716.1};
OS   OM182 bacterium BACL3 MAG-120619-bin3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM182 clade.
OX   NCBI_TaxID=1655593 {ECO:0000313|EMBL:KRO81716.1, ECO:0000313|Proteomes:UP000051242};
RN   [1] {ECO:0000313|EMBL:KRO81716.1, ECO:0000313|Proteomes:UP000051242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL22 MAG-120619-bin3 {ECO:0000313|EMBL:KRO81716.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C.,
RA   Pinhassi J., Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRO81716.1}.
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DR   EMBL; LICD01000074; KRO81716.1; -; Genomic_DNA.
DR   Proteomes; UP000051242; Unassembled WGS sequence.
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:UP000051242};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KRO81716.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KRO81716.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    134       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    154    174       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    181    198       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    218    246       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    258    282       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    117       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      128    239       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   284 AA;  30401 MW;  1D4B0ACF8E48A6B2 CRC64;
     MTLASALVSN PTLFLGFVAL LGLLVGSFIN VIVYRLPIML ERAWQSSELP TEAFNLAVPR
     SHCPSCAQQL SASENVPVVS FLFLRGRCRH CKSRISARYP LVEIAASVAS ILVAMTFGFT
     ASTLAFLAFA WFLLALSLID LDHHLLPDDL TLPLLWLGLL VSAFNLGLPG VSLFDAVIGA
     AAGYMTLWSL FWAFLLVTGK EGLGYGDFKL LAALGAWLGW QAILPVLLLA SLAGAVIGLI
     LIVFGGRERS APLPFGPFLA AAGFVMLIWG PQALALYGTL FAPH
//
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