ID A0A1H6XW11_9FLAO Unreviewed; 528 AA.
AC A0A1H6XW11;
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|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=SAMN05660918_0046 {ECO:0000313|EMBL:SEJ33229.1};
OS Flavobacterium terrigena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402734 {ECO:0000313|EMBL:SEJ33229.1, ECO:0000313|Proteomes:UP000199702};
RN [1] {ECO:0000313|EMBL:SEJ33229.1, ECO:0000313|Proteomes:UP000199702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17934 {ECO:0000313|EMBL:SEJ33229.1,
RC ECO:0000313|Proteomes:UP000199702};
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|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; FNYA01000010; SEJ33229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6XW11; -.
DR STRING; 402734.SAMN05660918_0046; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000199702; 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; IPR043739; DUF5684.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
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; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 126..288
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 388..468
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 528 AA; 60439 MW; 518CC2A5196DF298 CRC64;
MEITSWIITI LVISTIHAIC TWKLYVKAGR KAWEAFVPVY NGIVLMQIIN RPKWWMFLVF
LPVINLLILP VIWIETLRTF GKKTTADMWL GVITLGLYIG FVNYTQEVSY EANRETKPAT
KALDTLGSLT FALIVATFVH TYFIQPFVIP SASLEKSLLI GDFLFVSKFH YGARTPMTPI
AAPMVHDSIP KTGKLSYFSK PQLPYFRFPA LEKIKNNDIV VFNWPRDTLD NMYHPSPIRV
DKPRDKKTNY VKRCVGIPGD SLQIKDGIVF VNGKELILPE RAKPQYSYEV TYDANTSIDF
EGLLKELNST DGAGFKNEAR DTLYIQSLTF EGAEKLKTVS GIKTVNRVIN KGPEDGVFPD
FKDGKPSVTN NWSGDNFGPI YIPQAGKTVA LNKETLPLYK IIITEYEGNT LEVKGNEIKI
NGKPVTSYTF KQDYYWMMGD NRHNSLDARY FGYTPADHIV GKPIFIWMSL DWNAKGLMNK
FRTERFFTTV NGEGQPQSYF KYFLIVLGAY FVWDWFRGKK KKKETDLL
//
