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Database: UniProt
Entry: E0QSZ0_9ACTO
LinkDB: E0QSZ0_9ACTO
Original site: E0QSZ0_9ACTO 
ID   E0QSZ0_9ACTO            Unreviewed;       482 AA.
AC   E0QSZ0;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
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:EFM45329.1};
GN   ORFNames=HMPREF0580_2018 {ECO:0000313|EMBL:EFM45329.1};
OS   Mobiluncus mulieris ATCC 35239.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=871571 {ECO:0000313|EMBL:EFM45329.1, ECO:0000313|Proteomes:UP000003045};
RN   [1] {ECO:0000313|EMBL:EFM45329.1, ECO:0000313|Proteomes:UP000003045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35239 {ECO:0000313|EMBL:EFM45329.1,
RC   ECO:0000313|Proteomes:UP000003045};
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 (AUG-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:EFM45329.1}.
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DR   EMBL; AEET01000044; EFM45329.1; -; Genomic_DNA.
DR   RefSeq; WP_004012905.1; NZ_GL405260.1.
DR   AlphaFoldDB; E0QSZ0; -.
DR   STRING; 871571.HMPREF0580_2018; -.
DR   GeneID; 66608171; -.
DR   HOGENOM; CLU_565980_0_0_11; -.
DR   Proteomes; UP000003045; 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:EFM45329.1};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003045}.
FT   DOMAIN          244..441
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   482 AA;  52378 MW;  AA231CD602A01F96 CRC64;
     MDVSPKFSAD NGGTFPPGTG LPPDPRSDKQ SSGSTKGAAN SGTEGHNGRN LNPKGTGGAR
     GVDSSETQYF AEEFPRAHPG GEFPGGMTGR MPGAMPGEYP GYPPMYSAWN PDLGFGDYPP
     GLYDQLFEYY SNGAHPYSGR SDGKKTGSDA SHPEKGARSK VTQRAGSGKG ESKNPDNDDD
     LLWGDLNDFQ AVHQSDSNRD SVDEFRASRM MRPRAYPNPN ELMVRQAGAF GRPQLTLDFP
     WYFELIAVVI TMLTISSLVR TFLLQPFYIP SASMQNTLMV NDSVLVAKTA PRYSPLNRGD
     IVVFRDTENW LQSGREGLVK KKAPNPVLGG IKRFMIFAGL APEDAQGFVI KRVMGMGGDT
     VTCCDEDGLL NINGKAIDED YTLNTGVASE VKFNVVVPKG SLWVMGDNRN HSADSRYHMD
     SPSGGFVSEK QVVGRAFVVV WPLEHMRFIS PSCAFYNIPK PVLGDKDAFS SESNEVPPGR
     RG
//
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