ID A0A1K1LNZ0_9FLAO Unreviewed; 510 AA.
AC A0A1K1LNZ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN02927921_00133 {ECO:0000313|EMBL:SFW12600.1};
OS Sinomicrobium oceani.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sinomicrobium.
OX NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW12600.1, ECO:0000313|Proteomes:UP000182248};
RN [1] {ECO:0000313|EMBL:SFW12600.1, ECO:0000313|Proteomes:UP000182248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW12600.1,
RC ECO:0000313|Proteomes:UP000182248};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPJE01000001; SFW12600.1; -; Genomic_DNA.
DR RefSeq; WP_072315371.1; NZ_FPJE01000001.1.
DR AlphaFoldDB; A0A1K1LNZ0; -.
DR STRING; 1150368.SAMN02927921_00133; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000182248; 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; 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; 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:UP000182248};
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 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 487..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 123..287
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 377..460
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 152
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 510 AA; 59072 MW; 3DF00DB2EC8223F2 CRC64;
MTATAWFVFF LVLQVVHFAG TWKLYQKAGR KAWEALIPVY NAVILMKIVN RPWWWVVLLF
IPIINLIMFP VVWVETARSF GRNSTTDTWL TILSLGLYLY YINSLDVSHI PERSTKPATA
TGEWVSSILF AIVAATLVHT YIMQPYVIPT SSLEKSLLVG DFLFVSKFHY GARTPMTAVA
APMVHDTIPG LKIKSYLNKP QLPYFRFPAL QHIRRNDIVV FNWPTDTVRY FGDRRIPGVH
KPIDKKSNYV KRCVGIPGDS LRIRNGYVYI NGQRLQLPDR AKTQYSYLVK TKGGELSRSY
MYERFGVTDP FYQVGNNTYR FTALTEESAS RLEKNQNVVS VERRIASEGL PDPRIFPNTR
DKKWSTDNFG PIYIPKKGKT VTLNSESLPF YRRIIEEYEH HTLEEKGGHI LIDGQQTDAY
TFQQDYFWMM GDNRHNSEDS RYWGYVPEDH IVGKPVFIWM SWDNQGGGVR WERVFTTVGG
SGEPVSYLKY VLIVVAGWII FSFIRKKRKK
//
