ID A0A1T5KKK4_9BACT Unreviewed; 369 AA.
AC A0A1T5KKK4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=SAMN05660236_2302 {ECO:0000313|EMBL:SKC64200.1};
OS Ohtaekwangia koreensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Ohtaekwangia.
OX NCBI_TaxID=688867 {ECO:0000313|EMBL:SKC64200.1, ECO:0000313|Proteomes:UP000190961};
RN [1] {ECO:0000313|EMBL:SKC64200.1, ECO:0000313|Proteomes:UP000190961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25262 {ECO:0000313|EMBL:SKC64200.1,
RC ECO:0000313|Proteomes:UP000190961};
RA Peterson S.W.;
RL Submitted (FEB-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|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}.
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DR EMBL; FUZU01000001; SKC64200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5KKK4; -.
DR STRING; 688867.SAMN05660236_2302; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000190961; 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; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
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; PS00760; SPASE_I_2; 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:UP000190961};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 21..161
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 313..350
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 369 AA; 43413 MW; EB3B7895CA96AD6C CRC64;
MLLEKVEDIA APKETLRTLL WRSVRTILYT ALAIYIVSIF LIGNFKVTGP SMEGTLLEGD
RVLVSKLHYG ARIPRILQLP WIDHRNPLLE YLNLRLYSNP IIPYLRTGAL SSLTRGDIVV
FNLPMQEDTY EINEVINKRI VALPGDIISL EDGILYCNDQ REVTDAVSFR HDLRTRKKLD
AAGAKQWDIF DYRNQVRLIE NPFTKEYFQY DIYTTGLGAQ KIEKDTNVLK ITRRESDNFS
DFNAYPHWLP LHWNKDHFGK IMIPRKGLKL KMDADNIARY FPLIKNLEDN DRAEIRQGSL
YIDDKPIAEY QFRKDYYFAL GDNRDKSMDS RHWGFIPEDH IIGKVVLIYF SKDIYRNEIR
WKRIFQSPQ
//
