LEP4_BACSU
ID LEP4_BACSU Reviewed; 248 AA.
AC P15378;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Prepilin leader peptidase/N-methyltransferase;
DE AltName: Full=Late competence protein ComC;
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=comC; OrderedLocusNames=BSU28070;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2553669; DOI=10.1128/jb.171.11.6043-6051.1989;
RA Mohan S., Aghion J., Guillen N., Dubnau D.A.;
RT "Molecular cloning and characterization of comC, a late competence gene of
RT Bacillus subtilis.";
RL J. Bacteriol. 171:6043-6051(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 206.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 AND 181-248.
RC STRAIN=168 / PY79;
RX PubMed=8419299; DOI=10.1128/jb.175.2.528-540.1993;
RA Margolis P.S., Driks A., Losick R.;
RT "Sporulation gene spoIIB from Bacillus subtilis.";
RL J. Bacteriol. 175:528-540(1993).
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:P25960}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P22610};
CC Note=Zinc is required for the N-terminal methylation of the mature
CC pilin, but not for signal peptide cleavage.
CC {ECO:0000250|UniProtKB:P22610};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22610};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P22610}.
CC -!- INDUCTION: By several proteins including Spo0A, Spo0H, Sin, AbrB, DegS,
CC DegU, ComA, ComB and ComK.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. {ECO:0000305}.
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DR EMBL; M30805; AAA83365.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14767.2; -; Genomic_DNA.
DR EMBL; L04520; AAB59022.1; -; Genomic_DNA.
DR EMBL; L04519; AAB59025.1; -; Genomic_DNA.
DR PIR; A33490; A33490.
DR RefSeq; NP_390685.2; NC_000964.3.
DR RefSeq; WP_010886586.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P15378; -.
DR STRING; 224308.BSU28070; -.
DR MEROPS; A24.019; -.
DR PaxDb; P15378; -.
DR PRIDE; P15378; -.
DR EnsemblBacteria; CAB14767; CAB14767; BSU_28070.
DR GeneID; 936586; -.
DR KEGG; bsu:BSU28070; -.
DR PATRIC; fig|224308.43.peg.2932; -.
DR eggNOG; COG1989; Bacteria.
DR InParanoid; P15378; -.
DR OMA; VFWLFKL; -.
DR PhylomeDB; P15378; -.
DR BioCyc; BSUB:BSU28070-MON; -.
DR Proteomes; UP000001570; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR010627; Pept_A24A_N.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR Pfam; PF06750; DiS_P_DiS; 1.
DR Pfam; PF01478; Peptidase_A24; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Competence; Hydrolase; Membrane; Metal-binding;
KW Methyltransferase; Multifunctional enzyme; Protease; Reference proteome;
KW S-adenosyl-L-methionine; Sporulation; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..248
FT /note="Prepilin leader peptidase/N-methyltransferase"
FT /id="PRO_0000192616"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P22610"
FT CONFLICT 206
FT /note="A -> R (in Ref. 1; AAA83365 and 4; AAB59025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26435 MW; 5266453B73D26097 CRC64;
MLSILFIFGL ILGSFYYTAG CRIPLHLSII APRSSCPFCR RTLTPAELIP ILSFLFQKGK
CKSCGHRISF MYPAAELVTA CLFAAAGIRF GISLELFPAV VFISLLIIVA VTDIHFMLIP
NRILIFFLPF LAAARLISPL DSWYAGLLGA AAGFLFLAVI AAITHGGVGG GDIKLFAVIG
FVLGVKMLAA AFFFSVLIGA LYGAAAVLTG RLAKRQPLPF APAIAAGSIL AYLYGDSIIS
FYIKMALG
