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Database: UniProt
Entry: K2JLN8_9PROT
LinkDB: K2JLN8_9PROT
Original site: K2JLN8_9PROT 
ID   K2JLN8_9PROT            Unreviewed;       242 AA.
AC   K2JLN8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=P24_10760 {ECO:0000313|EMBL:EKE75332.1};
OS   Oceanibaculum indicum P24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Oceanibaculaceae; Oceanibaculum.
OX   NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE75332.1, ECO:0000313|Proteomes:UP000006746};
RN   [1] {ECO:0000313|EMBL:EKE75332.1, ECO:0000313|Proteomes:UP000006746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P24 {ECO:0000313|EMBL:EKE75332.1,
RC   ECO:0000313|Proteomes:UP000006746};
RX   PubMed=23209207; DOI=10.1128/JB.01859-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL   J. Bacteriol. 194:6942-6942(2012).
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:EKE75332.1}.
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DR   EMBL; AMRL01000012; EKE75332.1; -; Genomic_DNA.
DR   RefSeq; WP_008944758.1; NZ_AMRL01000012.1.
DR   AlphaFoldDB; K2JLN8; -.
DR   STRING; 1207063.P24_10760; -.
DR   MEROPS; S26.001; -.
DR   PATRIC; fig|1207063.3.peg.2177; -.
DR   eggNOG; COG0681; Bacteria.
DR   Proteomes; UP000006746; 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   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006746}.
FT   DOMAIN          9..213
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   242 AA;  27561 MW;  5438BD46CE342C96 CRC64;
     MSKSGGIGET IRTVVYAILI ALGIRTFAYE PFNIPSGSMI PTLLVGDYLF VSKFSYGYSR
     YSLPFGLPLI PGRILFTEPE RGDVVVFKLP RDNETDYIKR IVGLPGDRIR MVDGRLYINN
     ELVKRERIED FVPEEAPNVR VTQFIETLPN GRRHRILERS DNGMLDNTPE YVVPAGHYFG
     MGDNRDDSVD SRVLAGVGYI PRENLVGRAD VLFFSTNGTA ALWEIWKWPF AIRYDRLFDG
     IR
//
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