ID A0A2N3II66_9BACT Unreviewed; 402 AA.
AC A0A2N3II66;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=Rain11_0941 {ECO:0000313|EMBL:PKQ70004.1};
OS Raineya orbicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ70004.1, ECO:0000313|Proteomes:UP000233387};
RN [1] {ECO:0000313|EMBL:PKQ70004.1, ECO:0000313|Proteomes:UP000233387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ70004.1,
RC ECO:0000313|Proteomes:UP000233387};
RA Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL Submitted (JUN-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}.
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:PKQ70004.1}.
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DR EMBL; NKXO01000012; PKQ70004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3II66; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000233387; 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; 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; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
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:UP000233387};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 22..172
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 294..380
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 402 AA; 46754 MW; 37E906E8204D3A11 CRC64;
MRFIPSFFRK KDPNKPKKSK LREWIDAIVF AVVVATFLRW LLLEAYTIPT PSMEGSLLTG
DFLFVSKLHY GARTPKTPLQ VPLTHQKIFF TNIPSYLDWI QLPQYRLPHF SEVKNGDVVV
FNYPGFEEKQ PRHPVDLRTN YIKRCIAIAG DTLEIRNADV YVNGKRFPDH EKTQFSYSIE
VKDEIPQEDL EELGLFVGDD IENPDIEYLP AQNRYVGFLN AKTAEAISKL PQVKKVEKII
MPAGKKEEAG QTILNDKGKG ETIFGENVYP VFPHSAKFNW NRDNFGPLWV PKKGATIPIN
ETTLALYGFT IQEFEGYDKD ELEITNNNEL IIDKKPVKTY TFKQDYYFMM GDNRHNSLDS
RYWGFVPADH IVGKALFIWM SWESRAKWYK KIRWGRLFNG ID
//
