ID A0A2S5A3C2_9SPHI Unreviewed; 388 AA.
AC A0A2S5A3C2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 Name=lepB {ECO:0000313|EMBL:POY37036.1};
GN ORFNames=C3K47_08235 {ECO:0000313|EMBL:POY37036.1};
OS Solitalea longa.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=2079460 {ECO:0000313|EMBL:POY37036.1, ECO:0000313|Proteomes:UP000236893};
RN [1] {ECO:0000313|EMBL:POY37036.1, ECO:0000313|Proteomes:UP000236893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AV {ECO:0000313|EMBL:POY37036.1,
RC ECO:0000313|Proteomes:UP000236893};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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|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: 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:POY37036.1}.
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DR EMBL; PQVF01000005; POY37036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5A3C2; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000236893; 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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
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; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 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 Reference proteome {ECO:0000313|Proteomes:UP000236893};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 25..49
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 23..230
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 331..366
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 388 AA; 44526 MW; 29690E47A54B7F3E CRC64;
MKLLPKLFGK KKTAEVQKKS VVKEWFGAFM FALVMAGIIH TFFMQLFAVP TGSMEKNIMI
GDHLYVSKLN YGPRLPMTPV ALPLVHNTVP FTDNNSIFSS PVNAYSELIK LSYYRIPGTE
TLDRGEIVVF NWPVDKDAKG NFRPVDMKEH YVKRCVALPN DILEVKQGKL YVNNIATPMH
DQDQSSYLIA TNGNTFNKDF LKELGVREFS TEANANNDIL PVADNQYLMF LSKKQAELVA
KNPVVISITE YILPWNTRED DVFQPSNTNW NIDNYGPLTI PSKGATVELT LENLPLYQNI
ISIYEENQLK VENGLIYING QKASSYTFKL NYYFMMGDNR HNSLDSRSWG FVPEDHIVGK
PLFIYWSSND RGNFFDGVRW DRFFKKIE
//
