ID A0A2U9T775_9GAMM Unreviewed; 189 AA.
AC A0A2U9T775;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=C9I47_1097 {ECO:0000313|EMBL:AWV06814.1};
OS Lysobacter maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1605891 {ECO:0000313|EMBL:AWV06814.1, ECO:0000313|Proteomes:UP000249447};
RN [1] {ECO:0000313|EMBL:AWV06814.1, ECO:0000313|Proteomes:UP000249447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ9B {ECO:0000313|EMBL:AWV06814.1,
RC ECO:0000313|Proteomes:UP000249447};
RA Zhang X.-Q.;
RT "The complete genome of Lysobacter maris HZ9B, a marine bacterium
RT antagonistic against terrestrial plant pathogens.";
RL Submitted (MAY-2018) 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|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC pass 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP029843; AWV06814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9T775; -.
DR KEGG; lmb:C9I47_1097; -.
DR Proteomes; UP000249447; Chromosome.
DR GO; GO:0005886; C:plasma 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000249447};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 52..185
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 189 AA; 20754 MW; 1CCEEF459FAF7F49 CRC64;
MSEGRTEAWR RWLVRGLLSL AVLLPAAAIG MYLLNPLGAN SIDPRQRILG HAPYRMSSMG
MSPTLESGQI VIVRAGAYRA RGPERGDVVL FAHPEYGEHW LQRVIGLPGE TVSIEDCVLM
IDGRALGEDY VAPGRAVEDY SCRMAPLPVP QGQYLLMGDN RDNSMDGRMM GPIAEDTLVG
RVVRVLHAE
//
