ID A0A2S7TMJ3_9FLAO Unreviewed; 584 AA.
AC A0A2S7TMJ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=BSU00_01960 {ECO:0000313|EMBL:PQJ23048.1};
OS Tenacibaculum sp. SG-28.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=754426 {ECO:0000313|EMBL:PQJ23048.1, ECO:0000313|Proteomes:UP000239112};
RN [1] {ECO:0000313|Proteomes:UP000239112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-28 {ECO:0000313|Proteomes:UP000239112};
RA Kumagai Y., Yoshizawa S., Kogure K.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PQJ23048.1}.
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DR EMBL; MQVY01000001; PQJ23048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7TMJ3; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000239112; 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; 2.
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:UP000239112};
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 54..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 88..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 558..576
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..292
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 482..524
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 584 AA; 67665 MW; 41C1375EC2153F13 CRC64;
MTFIEWFIFF ILIQIIHFFG TWKLYVKAER KAWEAAVPIY NAIVLMGIIK RPKWWVILLF
VPIINLLMFP IVWIETCRSF GFNKGKDTVL AIVSLGFYIY YINYATNCTY RKDRSLKPPN
KVDEWLSSIA FAIIAATLVH TYFMQPYTIP TSSLEKTLLV GDYLFVSKFH YGARVPMTTV
AAPMAHDTIP ILGTKSFLSE DNPEKKNSWK NKLALPYMRL PGLQKIKRND IVVFSWPADT
TKTMWGDYSG KQTYKPIDKR TNYVKRCVGI PGDSLEVRNG YVYINGKQTV LPDRAKPQWN
FLVYAKTGLT TKRVKGFVNK EFQRKFIAKV TTQEEFNLIR RLPSLRGINQ NGNNEFELIT
NEDGISRQVI QNNNLNIREI TTKVRQITLT DEEANALRKE TGIDSVVKTI EPKGFYNPSI
FPHSPKYHWS TDNFGPIYIP KKGVTVALNS DSFPFYKEII ERYENNNLTT VGDTYYINGK
KATSYTFQQD YYWMMGDNRQ NSLDARNWGY VPFDHVVGKP VMIWLSWDPN TSNIVDKIKS
IRWERMFTTV GGEGKPVSYL WVVIALLVGY LLYGFISKKK KTTK
//
