ID F4C532_SPHS2 Unreviewed; 474 AA.
AC F4C532;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=Sph21_0424 {ECO:0000313|EMBL:ADZ77006.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77006.1};
RN [1] {ECO:0000313|EMBL:ADZ77006.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ77006.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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}.
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DR EMBL; CP002584; ADZ77006.1; -; Genomic_DNA.
DR AlphaFoldDB; F4C532; -.
DR STRING; 743722.Sph21_0424; -.
DR KEGG; shg:Sph21_0424; -.
DR PATRIC; fig|743722.3.peg.461; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
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; PS00760; SPASE_I_2; 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 Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 127..278
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 405..451
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 474 AA; 54384 MW; 98404C4D3F7C746A CRC64;
MLTAFLVVFF LGTQIGLWLL FVKAGRPGWE SLIPFYREYI ITKLTGRPWW WVILLVVPII
NLFIGIGLYI DFVRCFGRRS FLDQVGTIIV PFIVFPLWGA DKTVTYWGAS ATEEFKKKYP
YKKSATREWA DAIVFAVVAA TLIRTFLIEA YMIPSGSMER SLLTGDFLFV SKINYGPRLP
MTPIAFPFAH HTMPITGTKA YWDGLEMDYR RLPGLQKIKR NDVVVFNYPM EADAPFNRPV
DKRENYIKRA IGIPGDTISI VNAQVYVNGK QGITPVEGQL MYEVTTDGTD INLDRINDMR
IDGGSTGQAN QYVFYLTPSL ANTIKGWANV KEIKPLIYPK GTPEPTQDIF PQGSDWNRDN
YGPVIVPHQG WTVQLNEQTV PIYERAITIY EGHTFEKKGD GYYIDGAKAT SYTFKMNYYW
MMGDNRHNSL DSRFWGFVPE DHIVGKALFV WLSLDDKGSF FDKIRWNRIF MGIH
//
