LEP4_PECCC
ID LEP4_PECCC Reviewed; 279 AA.
AC P31712;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE AltName: Full=Pectic enzymes secretion protein OutO;
DE Includes:
DE RecName: Full=Leader peptidase;
DE EC=3.4.23.43 {ECO:0000250|UniProtKB:P22610};
DE AltName: Full=Prepilin peptidase;
DE Includes:
DE RecName: Full=N-methyltransferase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P22610};
GN Name=outO;
OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SCRI 193;
RX PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA Salmond G.P.C.;
RT "Molecular cloning and characterization of 13 out genes from Erwinia
RT carotovora subspecies carotovora: genes encoding members of a general
RT secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL Mol. Microbiol. 8:443-456(1993).
RN [2]
RP TOPOLOGY.
RX PubMed=8065262; DOI=10.1111/j.1365-2958.1994.tb01033.x;
RA Reeves P.J., Douglas P., Salmond G.P.C.;
RT "Beta-lactamase topology probe analysis of the OutO NMePhe peptidase, and
RT six other Out protein components of the Erwinia carotovora general
RT secretion pathway apparatus.";
RL Mol. Microbiol. 12:445-457(1994).
CC -!- FUNCTION: Plays a role in type II pseudopili formation by
CC proteolytically removing the leader sequence from substrate proteins
CC and subsequently monomethylating the alpha-amino group of the newly
CC exposed N-terminal phenylalanine. Substrates include proteins required
CC for biogenesis of the type II general secretory apparatus.
CC {ECO:0000250|UniProtKB:P22610}.
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:0000250|UniProtKB:P22610};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P22610}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P22610}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. {ECO:0000305}.
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DR EMBL; X70049; CAA49656.1; -; Genomic_DNA.
DR PIR; S32869; S32869.
DR AlphaFoldDB; P31712; -.
DR MEROPS; A24.A10; -.
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: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 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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Methyltransferase;
KW Multifunctional enzyme; Protease; S-adenosyl-L-methionine; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..279
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192619"
FT TOPO_DOM 1..16
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 17..35
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 124..130
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 150..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 183..185
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 205..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 215..233
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 234..236
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 255..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 277..279
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8065262"
SQ SEQUENCE 279 AA; 31131 MW; FB514747FF99B1EA CRC64;
MDDLREFAQL FPAWWFGALG VLGLIVGSFL NVVIYRLPIM LERRWRQDIE LETGVADPDT
RYNLWWPPSS CPHCQQAIAV KDNIPLFSWL WLRGRSRCCH QSVSVQYPLV EVITMLAFLA
AGLLWLPGMA LWGALILLSF LLVLTVIDIK TLLLPDELTL SLLWMGLLFN LSGTFVSLND
AVVGAMAGYL SLWLLYWAFK YATGKEALGY GDFKLLAALG AWLGWQALPN LVLVAALSGL
VVTLIWRGLR KEDTAKPLAF GPWLAIGGVF GMIMNGFNL
