ID W4M6Z5_9BACT Unreviewed; 252 AA.
AC W4M6Z5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ETSY2_23220 {ECO:0000313|EMBL:ETX05392.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX05392.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETX05392.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
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:ETX05392.1}.
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DR EMBL; AZHX01000960; ETX05392.1; -; Genomic_DNA.
DR AlphaFoldDB; W4M6Z5; -.
DR PATRIC; fig|1429439.4.peg.3955; -.
DR HOGENOM; CLU_057101_0_1_7; -.
DR Proteomes; UP000019140; 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 Reference proteome {ECO:0000313|Proteomes:UP000019140};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..96
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 108..210
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 252 AA; 27473 MW; 7CE582495BA72DE6 CRC64;
MLQWFTFHHG YAFILGCMIG SFANVCIHRL PWQQSLMLPP SHCPNCQQGL RPWHNIPIIS
YLLLRGRCAY CQTAISWRYP FVELLCGLLY IVLYEHFGLS LQGMIFTLLA TSLLIVSFID
LAYRIIPDVI TLPGIIAGLL ASTLVTSVGI GSALLGVVIG GGLFLLIAII SRGGMGGGDI
KLTAMIGAFL GWQGVFVTIF LAALSGAVSG LFLMAIKKKG RKDALPFGPF LALGALLALL
WGHEIVHWYL RV
//
