YDIL_BACSU
ID YDIL_BACSU Reviewed; 244 AA.
AC O05525; Q797D2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative membrane peptidase YdiL;
DE EC=3.4.-.-;
DE AltName: Full=Putative CAAX prenyl protease;
GN Name=ydiL; OrderedLocusNames=BSU06010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
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).
CC -!- FUNCTION: May function as endopeptidase which proteolytically removes
CC the C-terminal three residues of farnesylated peptides containing the
CC CAAX motif where C is cysteine, A is an aliphatic amino acid and X is
CC any amino acid. {ECO:0000250|UniProtKB:Q6LZY8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6LZY8};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6LZY8}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; D88802; BAA19725.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12420.1; -; Genomic_DNA.
DR PIR; E69787; E69787.
DR RefSeq; NP_388482.1; NC_000964.3.
DR RefSeq; WP_003234069.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O05525; -.
DR STRING; 224308.BSU06010; -.
DR MEROPS; G05.007; -.
DR PaxDb; O05525; -.
DR PRIDE; O05525; -.
DR DNASU; 938033; -.
DR EnsemblBacteria; CAB12420; CAB12420; BSU_06010.
DR GeneID; 938033; -.
DR KEGG; bsu:BSU06010; -.
DR PATRIC; fig|224308.179.peg.646; -.
DR eggNOG; COG1266; Bacteria.
DR InParanoid; O05525; -.
DR OMA; QMPIFIV; -.
DR PhylomeDB; O05525; -.
DR BioCyc; BSUB:BSU06010-MON; -.
DR Proteomes; UP000001570; Chromosome.
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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR InterPro; IPR003675; Rce1-like.
DR Pfam; PF02517; Rce1-like; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..244
FT /note="Putative membrane peptidase YdiL"
FT /id="PRO_0000390303"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 209
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 213
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
SQ SEQUENCE 244 AA; 27590 MW; 86B9841CD32B19EF CRC64;
MRKQYWFIIL TYIIMQFSAL IAIPLLFKFG YAGGQPTDEN MLHAQGLWSV ISFIACLVVV
LLILRTVPKE TLRNGQKDSI GLSILWAIAG FFIALFSQGI AGSIEYYVFG IGRESENTQA
ILDVIQAVPL MIIVSSIVGP ILEEIIFRKI IFGALYEKTN FFFAGLISSV IFGIVHADLK
HLLLYTAMGF TFAFLYARTK RIWVPIFAHL MMNTFVVIMQ LEPVRNYLEQ QSTQMQLIIG
GLFL
