ID Q5FHN0_EHRRG Unreviewed; 238 AA.
AC Q5FHN0;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
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 Name=lepB {ECO:0000313|EMBL:CAI27832.1};
GN OrderedLocusNames=ERGA_CDS_03800 {ECO:0000313|EMBL:CAI27832.1};
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI27832.1, ECO:0000313|Proteomes:UP000000533};
RN [1] {ECO:0000313|EMBL:CAI27832.1, ECO:0000313|Proteomes:UP000000533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel {ECO:0000313|EMBL:CAI27832.1,
RC ECO:0000313|Proteomes:UP000000533};
RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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}; 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}.
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DR EMBL; CR925677; CAI27832.1; -; Genomic_DNA.
DR RefSeq; WP_011155054.1; NC_006831.1.
DR AlphaFoldDB; Q5FHN0; -.
DR MEROPS; S26.001; -.
DR GeneID; 56785107; -.
DR KEGG; erg:ERGA_CDS_03800; -.
DR HOGENOM; CLU_028723_1_2_5; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000000533; 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; 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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}.
FT DOMAIN 8..211
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 238 AA; 27130 MW; E4DF1DCE472525EF CRC64;
MKKSFPVREF ISTFILATLT VLAIRVFLFE PFHIPSGSMK STLLVGDYIF VSKYSYGYSR
YSFPFYLPII KGRIFPKTPK PGDVVVFRPP KDPGLHYIKR VIGIPGDKVQ IINGFLYING
NKMQYKKVSD FIDEDDGKAI CRYLETLPNG NTHEVLDDIQ DSPLDNTPVY TVPEDHVFVL
GDNRDNSRDS RFITDVGYIP LKNIIGKAHV IALSFTKSKD GSFLPFKLRS DRVWHAIN
//