ID A0A1B2M1Y4_9GAMM Unreviewed; 285 AA.
AC A0A1B2M1Y4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BFG52_12195 {ECO:0000313|EMBL:AOA59033.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA59033.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA59033.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA59033.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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}; 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}.
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DR EMBL; CP016895; AOA59033.1; -; Genomic_DNA.
DR RefSeq; WP_067556617.1; NZ_CP016895.1.
DR AlphaFoldDB; A0A1B2M1Y4; -.
DR STRING; 1789224.BFG52_12195; -.
DR KEGG; ala:BFG52_12195; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000093391; 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; 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.
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:UP000093391};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 42..266
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 285 AA; 33196 MW; 138296D32797E8D0 CRC64;
MDFDFNLILV PLTLVFFVIW LLDKLVFKQR KTRGKGHENA IITWSYDFWP VMVVVLVLRS
FFYEPFNIPS ESMVPTLETG DFILVNKYQY GVRLPILNDK IINISEPKRG EVFVFRYPED
PKLNYIKRVI GIPGDHIVYK NGVLSVNGQP VVQEPVAFER SKDSIMEPIA YFKESLGEHQ
HLIRRNEQFN PLFASYADNL TSKMKQPYVS KTNRPLFLNS QGNEWEAVVK DHEYFAMGDN
REYSADSRYW GMVPAENLVG KAVYIWTHKE PGWNLPSFSR NSAIK
//
