ID H5Y499_9FIRM Unreviewed; 181 AA.
AC H5Y499;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ORFNames=DesyoDRAFT_2879 {ECO:0000313|EMBL:EHQ89927.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ89927.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ89927.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ89927.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-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: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane
CC protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CM001441; EHQ89927.1; -; Genomic_DNA.
DR RefSeq; WP_007784081.1; NZ_CM001441.1.
DR AlphaFoldDB; H5Y499; -.
DR STRING; 768710.DesyoDRAFT_2879; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_9; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000005104; Chromosome.
DR GO; GO:0005886; C:plasma 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000005104};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 15..171
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 181 AA; 20765 MW; 6224B43BF8D86309 CRC64;
MESSEKPKSS VRFLIELIEI VLIAFALSWV LRTYVIEARK IPTGSMLPTI QLEDRVIVDK
FFFKRFDHIS PGDIIVFHPP PSAHATDDYI KRVVGLAGDT VEIKNNKTYV NGQPLYEPYL
FETTMNDFSM TVVPNDYVFV MGDNRNNSAD SREWGFLPVE NITGRTLFRY WPIDQIGALA
R
//