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Database: UniProt
Entry: E6LY86_9ACTO
LinkDB: E6LY86_9ACTO
Original site: E6LY86_9ACTO 
ID   E6LY86_9ACTO            Unreviewed;       444 AA.
AC   E6LY86;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   Name=lepB {ECO:0000313|EMBL:EFU80300.1};
GN   ORFNames=HMPREF0388_0823 {ECO:0000313|EMBL:EFU80300.1};
OS   Mobiluncus curtisii ATCC 51333.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=887326 {ECO:0000313|EMBL:EFU80300.1, ECO:0000313|Proteomes:UP000005573};
RN   [1] {ECO:0000313|EMBL:EFU80300.1, ECO:0000313|Proteomes:UP000005573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51333 {ECO:0000313|EMBL:EFU80300.1,
RC   ECO:0000313|Proteomes:UP000005573};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU362042};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFU80300.1}.
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DR   EMBL; AEPY01000005; EFU80300.1; -; Genomic_DNA.
DR   RefSeq; WP_004009249.1; NZ_GL622340.1.
DR   AlphaFoldDB; E6LY86; -.
DR   HOGENOM; CLU_616509_0_0_11; -.
DR   Proteomes; UP000005573; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EFU80300.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        202..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          205..405
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..111
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   444 AA;  48036 MW;  D41E583B45580A55 CRC64;
     MTMPQQPENA NRDAPSSGTS PDGFNTNPQF AGAGTMPGSF PPGYEVFPGG IMPGEGAPYA
     PDGMGMPFPP EAFPGGYPSQ AAFPDGADFP GMDPNGMPPT QMPPGFPSPG MEPYPGMPYP
     PYGSIPFPGM MFDNEEIPDG SGKNGALAED DTDFKLDDEG SEFKSGRGAG MPGFRGMNAL
     PPGVRGNLDG LERPHLALDL PWYFEFIAVV ITALAISSLV RLFLLQPFYI PSQSMEKTLM
     INDSVLVNKF SARHGDINRG DIVVFEDVEG WSQTAAEQLR KRPPDRTPFQ IATKVKNFGI
     FVGLLPEDSQ GYLIKRVIGI PGDDVSCCDE DGLMTINGKA IDEDYIPQTG VSSDIEFSVV
     VPKNSLWVMG DNRPHSADSR WHQDKPSHGF VSESNVVGRA FVVVWPVERM KFITPSCAFY
     NIPKPATPND EFSSEADEAP PLTR
//
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