LEP4_XANCP
ID LEP4_XANCP Reviewed; 287 AA.
AC Q56763;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Prepilin leader peptidase/N-methyltransferase;
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=xpsO; Synonyms=pilD; OrderedLocusNames=XCC3101;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Xc1701;
RX PubMed=8817497; DOI=10.1111/j.1365-2958.1995.mmi_18040769.x;
RA Hu N.-T.T., Lee P.F., Chen C.;
RT "The type IV pre-pilin leader peptidase of Xanthomonas campestris pv.
RT campestris is functional without conserved cysteine residues.";
RL Mol. Microbiol. 18:769-777(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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: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; U12432; AAC43571.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM42372.1; -; Genomic_DNA.
DR PIR; S70810; S70810.
DR RefSeq; NP_638448.1; NC_003902.1.
DR RefSeq; WP_011038216.1; NC_003902.1.
DR AlphaFoldDB; Q56763; -.
DR STRING; 340.xcc-b100_1087; -.
DR MEROPS; A24.001; -.
DR EnsemblBacteria; AAM42372; AAM42372; XCC3101.
DR KEGG; xcc:XCC3101; -.
DR PATRIC; fig|190485.4.peg.3313; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_0_6; -.
DR OMA; VFWLFKL; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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 Cell inner membrane; Cell membrane; Hydrolase; Membrane; Methyltransferase;
KW Multifunctional enzyme; Protease; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..287
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192631"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 287 AA; 31843 MW; A58DD1A514F9ECC2 CRC64;
MAFLDQHPGL GFPAAAGLGL LIGSFLNVVI LRLPKRMEWQ WRRDAREILE LPDIYEPPPP
GIVVEPSHDP VTGDKLKWWE NIPLFSWLML RGKSRYSGKP ISIQYPLVEL LTSILCVASV
WRFGFGWQGF GAIVLSCFLV AMSGIDLRHK LLPDQLTLPL MWLGLVGSMD NLYMPAKPAL
LGAAVGYVSL WTVWWLFKQL TGKEGMGHGD FKLLAALGAW CGLKGILPII LISSLVGAVL
GSIWLFAKGR DRATPIPFGP YLAIAGWVVF FWGNDLVDGY LRFAGLR
