LEP4_ECOLI
ID LEP4_ECOLI Reviewed; 225 AA.
AC P25960; Q2M700;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE Includes:
DE RecName: Full=Leader peptidase;
DE EC=3.4.23.43 {ECO:0000269|PubMed:8655552};
DE AltName: Full=Prepilin peptidase;
DE Includes:
DE RecName: Full=N-methyltransferase;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P22610};
GN Name=gspO; Synonyms=hofD, hopD, hopO, yheC;
GN OrderedLocusNames=b3335, JW3297;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-225.
RC STRAIN=K12;
RX PubMed=2661540; DOI=10.1128/jb.171.7.3940-3947.1989;
RA Andrews S.C., Harrison P.M., Guest J.R.;
RT "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:3940-3947(1989).
RN [5]
RP IDENTIFICATION.
RX PubMed=1676385; DOI=10.1016/0378-1119(91)90221-v;
RA Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S.;
RT "Characterisation of a Pseudomonas aeruginosa twitching motility gene and
RT evidence for a specialised protein export system widespread in
RT eubacteria.";
RL Gene 101:33-44(1991).
RN [6]
RP LACK OF EXPRESSION, AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA Francetic O., Pugsley A.P.;
RT "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT 12 encodes functional proteins.";
RL J. Bacteriol. 178:3544-3549(1996).
RN [7]
RP LACK OF EXPRESSION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT "Expression of the endogenous type II secretion pathway in Escherichia coli
RT leads to chitinase secretion.";
RL EMBO J. 19:6697-6703(2000).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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:0000305|PubMed:8655552}.
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 -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC growth conditions. {ECO:0000269|PubMed:11118204}.
CC -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC in type II secretion machinery in other organisms, but is probably not
CC expressed under laboratory conditions. However, GspO is functional when
CC expressed from a stronger promoter (PubMed:8655552).
CC {ECO:0000305|PubMed:8655552}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. {ECO:0000305}.
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DR EMBL; L28106; AAC36928.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58132.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76360.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77956.1; -; Genomic_DNA.
DR EMBL; M27176; AAC13988.1; -; mRNA.
DR PIR; B65127; B65127.
DR RefSeq; NP_417794.1; NC_000913.3.
DR RefSeq; WP_000178154.1; NZ_LN832404.1.
DR AlphaFoldDB; P25960; -.
DR BioGRID; 4262465; 210.
DR STRING; 511145.b3335; -.
DR MEROPS; A24.A10; -.
DR PaxDb; P25960; -.
DR EnsemblBacteria; AAC76360; AAC76360; b3335.
DR EnsemblBacteria; BAE77956; BAE77956; BAE77956.
DR GeneID; 947840; -.
DR KEGG; ecj:JW3297; -.
DR KEGG; eco:b3335; -.
DR PATRIC; fig|1411691.4.peg.3396; -.
DR EchoBASE; EB1334; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_5_0_6; -.
DR InParanoid; P25960; -.
DR OMA; LAPAIWI; -.
DR PhylomeDB; P25960; -.
DR BioCyc; EcoCyc:EG11359-MON; -.
DR BioCyc; MetaCyc:EG11359-MON; -.
DR PRO; PR:P25960; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; IPR014032; Peptidase_A24A_bac.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR Pfam; PF01478; Peptidase_A24; 1.
DR PRINTS; PR00864; PREPILNPTASE.
PE 1: Evidence at protein level;
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..225
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192632"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..174
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..225
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 131
FT /note="A -> P (in Ref. 4; AAC13988)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="WL -> CV (in Ref. 2; AAA58132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24957 MW; 90297BB7E6592EDD CRC64;
MTMLLPLFIL VGFIADYFVN AIAYHLSPLE DKTALTFRQV LVHFRQKKYA WHDTVPLILC
VAAAIACALA PFTPIVTGAL FLYFCFVLTL SVIDFRTQLL PDKLTLPLLW LGLVFNAQYG
LIDLHDAVYG AVAGYGVLWC VYWGVWLVCH KEGLGYGDFK LLAAAGAWCG WQTLPMILLI
ASLGGIGYAI VSQLLQRRTI TTIAFGPWLA LGSMINLGYL AWISY
