GenomeNet

Database: UniProt
Entry: A0A1I3C084_9GAMM
LinkDB: A0A1I3C084_9GAMM
Original site: A0A1I3C084_9GAMM 
ID   A0A1I3C084_9GAMM        Unreviewed;       288 AA.
AC   A0A1I3C084;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=DFO67_10540 {ECO:0000313|EMBL:TDX30254.1},
GN   SAMN04487959_107259 {ECO:0000313|EMBL:SFH67975.1};
OS   Halomonas xianhensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH67975.1, ECO:0000313|Proteomes:UP000199040};
RN   [1] {ECO:0000313|EMBL:SFH67975.1, ECO:0000313|Proteomes:UP000199040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH67975.1,
RC   ECO:0000313|Proteomes:UP000199040};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TDX30254.1, ECO:0000313|Proteomes:UP000294489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6_TX {ECO:0000313|EMBL:TDX30254.1,
RC   ECO:0000313|Proteomes:UP000294489};
RA   Lamendella R.;
RT   "Freshwater and sediment microbial communities from various areas in North
RT   America, analyzing microbe dynamics in response to fracking.";
RL   Submitted (MAR-2019) 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   ---------------------------------------------------------------------------
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; FOPY01000007; SFH67975.1; -; Genomic_DNA.
DR   EMBL; SOEC01000005; TDX30254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3C084; -.
DR   STRING; 442341.SAMN04487959_107259; -.
DR   OrthoDB; 9789291at2; -.
DR   Proteomes; UP000199040; Unassembled WGS sequence.
DR   Proteomes; UP000294489; 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   ECO:0000313|EMBL:SFH67975.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199040};
KW   Transferase {ECO:0000256|RuleBase:RU003794, ECO:0000313|EMBL:SFH67975.1};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..123
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          138..244
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   288 AA;  31059 MW;  C952B20EF852357C CRC64;
     MSLNLPPVLL WPLVAILGLA LGSFVNVVIA RLPAMLMLQW RAEAREALEL PEEAPGSVLP
     RVNLATPRSS CPRCGEPIAW HDNIPLFGYL KRRGRCANCE KPISLRYPLV ELAGGALAVA
     VVALYGPTLA SLFVLGACLI LLALAVIDLR TQLLPDVLTL PLLWLGLLYQ VLFQPLLLQS
     AVIGAVAGYL VLWSFYWLFK LITGKEGMGY GDFKLLAALG AWTGWEMLPL LLILSAGVGA
     VVGILSQLAL PRLRGMPMPF GPFLAMAGWI ALLFGAPLMA VYQAILLS
//
DBGET integrated database retrieval system