ID A0A0K1NFM9_9BURK Unreviewed; 322 AA.
AC A0A0K1NFM9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ADJ79_12715 {ECO:0000313|EMBL:AKU67855.1};
OS Ottowia sp. oral taxon 894.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU67855.1, ECO:0000313|Proteomes:UP000056623};
RN [1] {ECO:0000313|Proteomes:UP000056623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP012073; AKU67855.1; -; Genomic_DNA.
DR RefSeq; WP_050716271.1; NZ_CP012073.1.
DR AlphaFoldDB; A0A0K1NFM9; -.
DR STRING; 1658672.ADJ79_12715; -.
DR KEGG; oto:ADJ79_12715; -.
DR PATRIC; fig|1658672.3.peg.3253; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000056623; 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 Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 97..310
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 322 AA; 36509 MW; 8AC42B43B5C2C8D9 CRC64;
MPALTAFILA ALAGYCVAWY AGYIEGNFPL LLLVATVITG AYWLAERFFF LPRRRAAASA
LEARHDARRA ELAAQGISQV DADISEARER LLSQPWWLDW TAGLFPIILA VFLLRSFVFE
PFRIPSGSMI PTLRIDDLIL VNKFTYGIRL PVFNTRVTQG NPIQRGDVVV FHYPLQPSLD
YIKRVVGLPG DEVTYLNKQI TVNGQPVPQT PDGEFLDKST VQYFRQIQET PAPGKQHSII
VDDQRPTLIP SVTQFPHRDL CQYSIEGVRC KVPPGHYFMM GDNRDNSLDS RYWGFVPDDY
IVGKAFFVWM NIGDLSRIGF FN
//
