ID A0A1G8G3M5_9FLAO Unreviewed; 535 AA.
AC A0A1G8G3M5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04489796_10584 {ECO:0000313|EMBL:SDH88982.1};
OS Winogradskyella thalassocola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=262004 {ECO:0000313|EMBL:SDH88982.1, ECO:0000313|Proteomes:UP000199492};
RN [1] {ECO:0000313|EMBL:SDH88982.1, ECO:0000313|Proteomes:UP000199492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15363 {ECO:0000313|EMBL:SDH88982.1,
RC ECO:0000313|Proteomes:UP000199492};
RA de Groot N.N.;
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: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}.
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DR EMBL; FNCZ01000005; SDH88982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8G3M5; -.
DR STRING; 262004.SAMN04489796_10584; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000199492; 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; 2.
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 53..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 509..526
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..291
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 398..477
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 535 AA; 62030 MW; C024A5DF2F23D22D CRC64;
MSWTQWFIFL LIIQIIHGLG TWKLYIKAGR QAWEAFVPVY NAVVLMKIIS RPWWWVILMF
LPIVNLIMIP AVWVETARSF GKDSKIDALL CIVTLGFYLF YLNYAADVNY IENRELKPKT
SSGEWISSIL FAVVAATIVH TYFFQPFVIP SSSLEKSLLV GDFLIVSKFH YGARTPMTTV
GAPMVHDTIP VLGKKSYLYN DNFEERNTSW INKLQLPFFR FPGFENVERN DIVVFNQPAD
TLLNMNDFNP DRNYYKPIDK KTNLVKRCVG IAGDTLEIRN GYVFINGKQN KLPPRSHLQF
SYDITFKRQL QPLRIIDILK KYDITDHLGY GTTEGSYSIP AATDEAIAKL RLHPEVASIV
PTKQVKGVDG NIFPRDKNYP WNTDYFGPMW IPKAGGTVNL TTENISIYKR AISEYEGHKV
VTRGNQIFID DQPATSYTFQ QDYYWMMGDN RHNSVDSRYW GFVPNDHIFG KPVFIWMSID
GINDGIKNWS FRWDRIFTTV TGPNERTSYL IPFIIFIVGL TFFNKWRRKK KAKQS
//
