ID E6WUA6_PSEUU Unreviewed; 266 AA.
AC E6WUA6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Psesu_1989 {ECO:0000313|EMBL:ADV27826.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27826.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV27826.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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}; Multi-
CC pass 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP002446; ADV27826.1; -; Genomic_DNA.
DR RefSeq; WP_013535654.1; NC_014924.1.
DR AlphaFoldDB; E6WUA6; -.
DR STRING; 743721.Psesu_1989; -.
DR MEROPS; S26.001; -.
DR KEGG; psu:Psesu_1989; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_1_6; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000008632; Chromosome.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ADV27826.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 45..244
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 266 AA; 29888 MW; ACCA8C7F7AC82981 CRC64;
MKWFEIGLVV LTFATGIIWL LDRLFFARRR AATAGLLDEE PAVVDYSRAF FPVLAAVLVL
RSFIAEPYKI PSSSMMPNLL IGDFILVNKF SYGLRLPVNN HKVVALGEPA RGDVVVFKPP
HDPDQNWIKR VVGLPGDQIA FRGDTLYING EAMRYTPIGE YVGQGRGAEM NGATLLTEHL
PGRDHSVLEW IDRAAPSGQG EWTVPEGHYF VMGDNRDNSE DSRFWTQTHF LPEENLRGKA
FLIWLNCEGW FCTGSFDPSR IGTSIK
//
