ID A0A1E8E2L4_9GAMM Unreviewed; 275 AA.
AC A0A1E8E2L4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BJN41_05145 {ECO:0000313|EMBL:OFE43744.1};
OS Acinetobacter towneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=202956 {ECO:0000313|EMBL:OFE43744.1, ECO:0000313|Proteomes:UP000186931};
RN [1] {ECO:0000313|EMBL:OFE43744.1, ECO:0000313|Proteomes:UP000186931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2Ac02 {ECO:0000313|EMBL:OFE43744.1,
RC ECO:0000313|Proteomes:UP000186931};
RA Barbosa B., Fernandez-Garcia L., Gato E., Leao R., Albano R., Fernandez B.,
RA Fernandez-Cuenca F., Marques E., Tomas M.;
RT "Genome of airborne Acinetobacter sp. 5-2Ac02 in the hospital environment:
RT Species near to Acinetobacter towneri.";
RL Submitted (OCT-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}.
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:OFE43744.1}.
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DR EMBL; MKQS01000009; OFE43744.1; -; Genomic_DNA.
DR RefSeq; WP_019837689.1; NZ_MKQS01000009.1.
DR AlphaFoldDB; A0A1E8E2L4; -.
DR STRING; 202956.BJN41_05145; -.
DR eggNOG; COG0681; Bacteria.
DR Proteomes; UP000186931; 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; 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 Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 39..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 42..257
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 275 AA; 31597 MW; ED061FB187E924C6 CRC64;
MDFDFNLILV PATLFFIVVW LLDKFVFKQR ATKGRGNENF IITWAYDFWP VLAVVMVLRS
FLYEPFNIPS DSMVPTLETG DFILVNKFEY GVRLPIINSK IIDVGSPERG EVAVFRYPPQ
PSISYIKRIV GLPGDHIVYD HGQLSINGKK VTKTPIQFSR EKDSLDTPTS IYHQETLGTH
TFTMRELEGV NVARQAPFLN YVDNGKYSAE NGLYWEVKVP DGHYFAMGDN RDQSADSRFW
GFVPEENLTG RAFYIWMHKE PGFNLPSFSR NGKID
//
