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Database: UniProt
Entry: A0A259FH56_9PROT
LinkDB: A0A259FH56_9PROT
Original site: A0A259FH56_9PROT 
ID   A0A259FH56_9PROT        Unreviewed;       283 AA.
AC   A0A259FH56;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Prepilin leader peptidase/N-methyltransferase {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=B7X87_09995 {ECO:0000313|EMBL:OZA37814.1};
OS   Hydrogenophilales bacterium 17-64-34.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970527 {ECO:0000313|EMBL:OZA37814.1, ECO:0000313|Proteomes:UP000216129};
RN   [1] {ECO:0000313|EMBL:OZA37814.1, ECO:0000313|Proteomes:UP000216129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-64-34 {ECO:0000313|EMBL:OZA37814.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an essential role in type IV pili and type II
CC       pseudopili formation by proteolytically removing the leader sequence
CC       from substrate proteins and subsequently monomethylating the alpha-
CC       amino group of the newly exposed N-terminal phenylalanine.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-terminal,
CC         basic peptide of 5-8 residues from type IV prepilin, and then N-
CC         methylates the new N-terminal amino group, the methyl donor being S-
CC         adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={ECO:0000256|RuleBase:RU003794};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZA37814.1}.
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DR   EMBL; NCIL01000007; OZA37814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259FH56; -.
DR   Proteomes; UP000216129; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1220; -; 1.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   InterPro; IPR010627; Prepilin_pept_A24_N.
DR   PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE_N-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1.
DR   Pfam; PF06750; A24_N_bact; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003794};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..121
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          133..241
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   283 AA;  30277 MW;  38864B2A560C65E2 CRC64;
     MSLLTAEPAL FAGLVFLLGL LVGSFLNVVV HRLPKMMEAE WQAQCAELRG EALAEAGPYN
     LATPRSACPA CGHMITAREN IPILSWLLLR GRCSACGTAI SARYPLVELL TGLLSAGVAW
     KWGVSLETLG ALMLVWALIA LAFIDLDTTL LPDSLTLPLI WLGLLFNLHG HFADLPSAVI
     GAVAGYLVLW SVYWLFKLAT GKDGMGFGDF KLLAAIGAWL GWQMLPVTLL LSSVVGAAIG
     IAMVVFVKHD RRVPIPFGPY LAGGGLVALF FGADLTRAYL AQF
//
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