LEP4_HAEIN
ID LEP4_HAEIN Reviewed; 230 AA.
AC P44620;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=hofD; Synonyms=hopD; OrderedLocusNames=HI_0296;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
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; L42023; AAC21960.1; -; Genomic_DNA.
DR PIR; C64060; C64060.
DR RefSeq; NP_438463.1; NC_000907.1.
DR RefSeq; WP_005694370.1; NC_000907.1.
DR AlphaFoldDB; P44620; -.
DR STRING; 71421.HI_0296; -.
DR EnsemblBacteria; AAC21960; AAC21960; HI_0296.
DR KEGG; hin:HI_0296; -.
DR PATRIC; fig|71421.8.peg.312; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_105394_0_0_6; -.
DR OMA; LDWHYQL; -.
DR PhylomeDB; P44620; -.
DR BioCyc; HINF71421:G1GJ1-314-MON; -.
DR Proteomes; UP000000579; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR Pfam; PF01478; Peptidase_A24; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..230
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192633"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 230 AA; 26789 MW; CD12ABE9B74818D0 CRC64;
MIYFTMFLLG GILGIALWFY LSGFITRLQQ NIYAIYVELF PQNRSPFQPH FASIQQKKCG
HILRYFFSIG VGFIFLQIAF KDSIFTVWIG LTLIILWTIS YLDWHYQLIS TTPCLWLLTL
GLFGADNNFS LLTLSESIKS AASFFIVFYV IYWLAKFYYG KEAFGRGDYW LAMALGSFIH
LETLPHFLLL ASVLGICFSL IHRKKKEFLP FAPFMNLSAV IIYFVKYYGY
