ID D1KC80_9GAMM Unreviewed; 290 AA.
AC D1KC80;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=Sup05_0324 {ECO:0000313|EMBL:EEZ80253.1};
OS uncultured Candidatus Thioglobus sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus;
OC environmental samples.
OX NCBI_TaxID=655186 {ECO:0000313|EMBL:EEZ80253.1, ECO:0000313|Proteomes:UP000009383};
RN [1] {ECO:0000313|EMBL:EEZ80253.1, ECO:0000313|Proteomes:UP000009383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19900896; DOI=10.1126/science.1175309;
RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., Tringe S.G.,
RA Tortell P.D., Hallam S.J.;
RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic dead
RT zones.";
RL Science 326:578-582(2009).
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:RU003993};
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}.
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DR EMBL; GG729998; EEZ80253.1; -; Genomic_DNA.
DR AlphaFoldDB; D1KC80; -.
DR STRING; 655186.Sup05_0324; -.
DR MEROPS; S26.001; -.
DR PATRIC; fig|655186.3.peg.802; -.
DR Proteomes; UP000009383; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-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; PS00501; SPASE_I_1; 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:RU003993};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000009383};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 72..274
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 164
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 290 AA; 33343 MW; 9EE00E1215DE9CD2 CRC64;
MTIENASPFF AWDVSSYLAL FLVVAFIIVV VDQVFVSRAE EAKEKSFVGR WIYFICFLKF
KKGEKYLHRP KWVQWSAEFY PVLLLVFLLR GFIVEPFRIP SNSMMPTLLT GDFILVSKFD
YGVSLPVLNK KVIEFSKPKR GDVIVFRYPN YEKDSKYNGA DFIKRVVGIP GDQISYSSDH
LRINGNKVHY KDLGTYQGVE SGSGMTGFKH KRELLDDNSH DVLLDPNAHS KGVKLKVPQG
HYFVMGDNRA RSSDSRFWGF VPEEYIIGKA FGIWMHYDDS LKLDRVGGFD
//
