ID A0A0C1FAT7_9FLAO Unreviewed; 517 AA.
AC A0A0C1FAT7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=OA85_12215 {ECO:0000313|EMBL:KIA85164.1};
OS Flavobacterium sp. AED.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA85164.1, ECO:0000313|Proteomes:UP000031403};
RN [1] {ECO:0000313|EMBL:KIA85164.1, ECO:0000313|Proteomes:UP000031403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AED {ECO:0000313|EMBL:KIA85164.1,
RC ECO:0000313|Proteomes:UP000031403};
RA Gale A.N., Newman J.D.;
RT "Flavobacterium sp. AED Genome.";
RL Submitted (OCT-2014) 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:RU362042};
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}.
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:KIA85164.1}.
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DR EMBL; JSYM01000003; KIA85164.1; -; Genomic_DNA.
DR RefSeq; WP_039110059.1; NZ_JSYM01000003.1.
DR AlphaFoldDB; A0A0C1FAT7; -.
DR STRING; 1423323.OA85_12215; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000031403; 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; 2.
DR InterPro; IPR043739; DUF5684.
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; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00761; SPASE_I_3; 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 Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 490..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..283
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 417..459
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 517 AA; 59830 MW; B71CE80C45537610 CRC64;
MTLYQWFVFF LLVQIIHFLG TWKLYEAAGR KRWEAAIPVY NAIVLMKIIG RPTWWTILLF
IPIINLIMFP VIWVETLRSF GKRTSLDTFL GIITFGFYIY YINYTQKLDY VTDRSLQPEN
KTADTISSLL FAIIVATLVH TYFIQPYTIP TSSLEKSLLI GDFLFVSKMN YGARVPMTTV
ALPMVHDSIP LTKSKSYLSW PQLPYFRLPG IQNINRTDIV VFNWPVDTVY KFFDTSKRRA
YKPVDKKSNY VKRCVGIPGD SLSIKDGIVY INGTILQLPE RAKPQFSYAV ALDKKTPIDF
ESLLKELDVT DDAGFKSDLR DTLFLKALTA AGAERLKNVP GVVSVTRQIS KGVEDGIFPH
INKWNRDNFG PIYIPQKGKT VALTTETLPF YRMIISEYEK KDLKVNGSEI RIDGKVVNSY
TFDQNYYWMM GDNRHNSEDS RYWGYVPEDH IVGKPIFIWL SIDPHGKGLN KIRWDRVFTT
VSGEGQPQSY FKLFLLALVA FFVGEYFWKK RKEKKDL
//
