ID A0A238U9H8_9FLAO Unreviewed; 522 AA.
AC A0A238U9H8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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=TJEJU_1487 {ECO:0000313|EMBL:SNR15218.1};
OS Tenacibaculum jejuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=584609 {ECO:0000313|EMBL:SNR15218.1, ECO:0000313|Proteomes:UP000215214};
RN [1] {ECO:0000313|EMBL:SNR15218.1, ECO:0000313|Proteomes:UP000215214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: KCTC 22618 {ECO:0000313|Proteomes:UP000215214};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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; LT899436; SNR15218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238U9H8; -.
DR KEGG; tje:TJEJU_1487; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000215214; Chromosome tjeju.
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; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:SNR15218.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000215214};
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 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..302
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 392..472
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 522 AA; 60081 MW; 2280DEDA362A9273 CRC64;
MSFTGWFILF LIIQFIHFLG TWKLYVKAGR KAWEAAVPVY NAIVLLGILK RPKWWVILLF
VPTVNLIMFP VIWIETCRSF GFKSTKDSIL VIATLGFYIF YISYFNDPQY DQKRALKAPT
TAGEWVSSIA FAIVAATIVH NYFIRPYVIP SSSLEKTLLV GDYLFVSKFH YGSRVPMTTV
SLPMIHDSIP GLGTKSYVFS DDYENRNNSL INKLQLPYMR LPGLKKIKRN DIVVFGQPAD
TLRNMNILTS DRNYYKPIDK KTNLVKRCVG IAGDSLEIKD GYIYINGKRT VLPKSAKPQW
NFIVDTNGEK LSPGDLKRYN IREAKVFNDG RFYLTLTDAE AAALKKNPKV KSIEKSNRPK
GYYDDGIFPH NPKYPWSIDN FGPIYIPKKG ATVALNAESI PFYKRIIQEY EKNELTFFGD
DIYINGKKTD SYTFKQDYYW MMGDNRQNSL DARAWGYVPF DHVIGTPVMV WFSYDKDTGS
IRWDRMFTTV TNGESKSYFW LGIIAALAIL GFVFMPKKKK AK
//