ID C1DXV8_SULAA Unreviewed; 236 AA.
AC C1DXV8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN Name=lepB {ECO:0000313|EMBL:ACN98599.1};
GN OrderedLocusNames=SULAZ_0224 {ECO:0000313|EMBL:ACN98599.1};
OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium.
OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN98599.1, ECO:0000313|Proteomes:UP000001369};
RN [1] {ECO:0000313|EMBL:ACN98599.1, ECO:0000313|Proteomes:UP000001369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC {ECO:0000313|Proteomes:UP000001369};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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 -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP001229; ACN98599.1; -; Genomic_DNA.
DR RefSeq; WP_012673921.1; NC_012438.1.
DR AlphaFoldDB; C1DXV8; -.
DR STRING; 204536.SULAZ_0224; -.
DR MEROPS; S26.025; -.
DR KEGG; saf:SULAZ_0224; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_2_0; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000001369; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:ACN98599.1};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000001369};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 13..217
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 236 AA; 27044 MW; D9C7C0869C5A4550 CRC64;
MEGVDNKKKT NIKHIVETIV VIFVVVSLVR VFLVQAFNIP SGSMKPTLLV GDFILVNKLV
YGNWDIGIPF TSITFYHHNN RLAKIDRGDV IVFKYPEDPS IDFIKRVIAL PGDIVEVKND
IVYINGKPLK REEDGYYEDT NEKVKKYKET TVRSDGKEYS YTVMEIEDGI GPDFGPVKVP
PNSYFVMGDN RDNSKDSRFW GFVPDDYVIG QAFVIYFSID LRKPSIRIDR LGKVIY
//
