ID A0A0F3IUV1_9PROT Unreviewed; 250 AA.
AC A0A0F3IUV1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=VZ95_04520 {ECO:0000313|EMBL:KJV10486.1};
OS Elstera litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Elstera.
OX NCBI_TaxID=552518 {ECO:0000313|EMBL:KJV10486.1, ECO:0000313|Proteomes:UP000033774};
RN [1] {ECO:0000313|EMBL:KJV10486.1, ECO:0000313|Proteomes:UP000033774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dia-1 {ECO:0000313|EMBL:KJV10486.1,
RC ECO:0000313|Proteomes:UP000033774};
RA Rahalkar M.C., Dhakephalkar P.K., Pore S.D., Arora P., Kapse N.G.,
RA Pandit P.S.;
RT "Draft genome sequence of Elstera litoralis.";
RL Submitted (MAR-2015) 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: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}.
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:KJV10486.1}.
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DR EMBL; LAJY01000089; KJV10486.1; -; Genomic_DNA.
DR RefSeq; WP_045774816.1; NZ_LAJY01000089.1.
DR AlphaFoldDB; A0A0F3IUV1; -.
DR PATRIC; fig|552518.3.peg.4668; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000033774; 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:UP000033774};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 17..223
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 48
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 250 AA; 28325 MW; 08950332562C7C85 CRC64;
MKLGVSNKAT ASKANSWWDV IRQVTIAIVI ALGIRSFFAE PFNIPSGSMI PTLLVGDYVF
VTKYSYGYSR HSFPLSPPIF SGRTSDTLPA RGDVAVFKTP QDNKTDYIKR VVGLPGDRVQ
MREGRLYIND KLVDRRFVED YVYRTESGYT IRTRRYEETL PGNRKHTIIE QSDAGPLDNT
RVYEVPAGHL FMMGDNRDGS EDSRASVGFV PVENLVGKAQ VIWLSVDGSL FRFWELPWTL
RFNRIGQGLD
//
