ID A0A1E5AE86_9RHOB Unreviewed; 278 AA.
AC A0A1E5AE86;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=AB838_10755 {ECO:0000313|EMBL:OED48400.1};
OS Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED48400.1, ECO:0000313|Proteomes:UP000094333};
RN [1] {ECO:0000313|EMBL:OED48400.1, ECO:0000313|Proteomes:UP000094333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB1-7 {ECO:0000313|EMBL:OED48400.1};
RX PubMed=27681823; DOI=10.1038/srep34362;
RA Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT "Single sample resolution of rare microbial dark matter in a marine
RT invertebrate metagenome.";
RL Sci. Rep. 6:34362-34362(2016).
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}; 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OED48400.1}.
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DR EMBL; MDLF01000063; OED48400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5AE86; -.
DR STRING; 1868286.AB838_10755; -.
DR Proteomes; UP000094333; 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; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 11..254
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 278 AA; 30669 MW; 6DEFB121A5FF4585 CRC64;
MTAKAKTSSS IIETIKTVVY ALLIAGVFRT LFFQPFWIPS GSMKETLLIG DFLFVNKVAY
GYSYASCPSL RLPAIGVNID AKDVCSFLDG DNTRLLGSEP ERGDVAVFRH PVNGHDFIKR
LIGLPGDTVQ MKNGVLFING EPVKLQDAGA FEEVMERQGP QGSMPRCENA PVGQGAICKK
SRQIETLPGG SEHTVLNITN QGVDHTSVYH VPEGHYFFMG DNRDNSSDSR LPQTAGGVGF
VPYENLIGRA DRIMFSSAGR SMLYFWTWRS NRFFKGIQ
//