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Database: UniProt
Entry: A0A0B8T8S7_9SPHI
LinkDB: A0A0B8T8S7_9SPHI
Original site: A0A0B8T8S7_9SPHI 
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}.
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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
//
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