ID A0A0B8T8S7_9SPHI Unreviewed; 474 AA.
AC A0A0B8T8S7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=DI53_1878 {ECO:0000313|EMBL:KGE14355.1};
OS Sphingobacterium deserti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE14355.1, ECO:0000313|Proteomes:UP000031802};
RN [1] {ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA Zhang W.;
RT "Whole-Genome optical mapping and complete genome sequence of
RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT west of China.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE14355.1, ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX PubMed=25830331;
RA Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA Zhang W., Lin M.;
RT "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT Desert of China.";
RL PLoS ONE 10:E0122254-E0122254(2015).
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 -!- 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:KGE14355.1}.
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; JJMU01000027; KGE14355.1; -; Genomic_DNA.
DR RefSeq; WP_037498014.1; NZ_JJMU01000027.1.
DR AlphaFoldDB; A0A0B8T8S7; -.
DR STRING; 1229276.DI53_1878; -.
DR PATRIC; fig|1229276.3.peg.1932; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000031802; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000031802};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 5..21
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 81..99
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..273
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 368..452
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; 54607 MW; 8F50C9A5F76D51E4 CRC64;
MWYSIIAIWT IASIYGLWLL FKKAGREGWE AAVPFYREFV MAKLTGRPTW WIALLLVPIV
NIFIFYALYL DLLRSFGKRR FWETVVAVLL PFIFLPLWGH DAEVKYLGVA NSDAFRSKYP
YTKSVLREWA DAIVFATVAA TLIRGFLLEA YMIPTGSMER RLLIGDFLFV SKLNYGPRVP
ITPLAFPFAH HTMPITGGKA YSEWIQLPYK RLPGFQELKR NDVVVFNLPT EADPPYSRPV
DKRENYIKRA VGVPGDKVEM RKGELLVNGK DSYDSNDLQR AYLIYTDGSG LNLQQLVDKR
IDYAKDPADG LPFAEPYLLY VTGEEIADIA TWSNVKEILP YDNSGSAFPH SPSEKWDYHN
FGPIIIPKKG DVVQLTSQNL PLYDRIIRVY EANSLENRAD GIYVNNLKTD SYEIKMNYYW
MMGDNRDNSA DSREFGFVPE DHIVGKALFT WMSYDVDGTF LTKIRWNRIF KGIK
//