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Database: UniProt
Entry: A0A1H3FTE8_9BURK
LinkDB: A0A1H3FTE8_9BURK
Original site: A0A1H3FTE8_9BURK 
ID   A0A1H3FTE8_9BURK        Unreviewed;       288 AA.
AC   A0A1H3FTE8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
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=SAMN04515617_108155 {ECO:0000313|EMBL:SDX94221.1};
OS   Collimonas sp. OK242.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDX94221.1, ECO:0000313|Proteomes:UP000198586};
RN   [1] {ECO:0000313|EMBL:SDX94221.1, ECO:0000313|Proteomes:UP000198586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK242 {ECO:0000313|EMBL:SDX94221.1,
RC   ECO:0000313|Proteomes:UP000198586};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNOR01000008; SDX94221.1; -; Genomic_DNA.
DR   Proteomes; UP000198586; 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:UP000198586};
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   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      6     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    122    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    159    177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    220    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    261    280       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    126       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      136    245       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   288 AA;  31136 MW;  E96C20693F224EA3 CRC64;
     MQDGIFFLAA GSLLPTALAA VFGLLIGSFL NVVIHRLPIM MQRESDNYVA HESGKPLPHT
     ERYNLVVPRS ACPHCKRQIG ALENVPVLSY LALRGKCAGC KTPISVRYPL VEALSGGLSA
     LLIWHFGSGW LGLSTLVFVY LLIAMTFIDA DTQLLPDDLT LPLLWIGLLL NLSGLFVPLQ
     DAVIGAAAGY LSLWAIYWAF KLLTGKEGMG YGDFKLLAAL GAWLGWKMLP IIILLSSLVG
     AAVGIALIVF TRRGRDKPIP FGPYLAGAGL LAMLYGRTIL ETYFGFAT
//
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