(data stored in SCRATCH zone)

SWISSPROT: D4YYR7_SPHJU

ID   D4YYR7_SPHJU            Unreviewed;       297 AA.
AC   D4YYR7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   Name=lepB {ECO:0000313|EMBL:BAI95499.1};
GN   OrderedLocusNames=SJA_C1-06650 {ECO:0000313|EMBL:BAI95499.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95499.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95499.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC       {ECO:0000256|RuleBase:RU362042}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042};
CC       Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; AP010803; BAI95499.1; -; Genomic_DNA.
DR   RefSeq; WP_013039194.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06650; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; BAI95499; BAI95499; SJA_C1-06650.
DR   GeneID; 29272338; -.
DR   KEGG; sjp:SJA_C1-06650; -.
DR   eggNOG; ENOG4105C3F; Bacteria.
DR   eggNOG; COG0681; LUCA.
DR   HOGENOM; HOG000003673; -.
DR   KO; K03100; -.
DR   OMA; VECCDDQ; -.
DR   OrthoDB; POG091H023R; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYR7.
DR   SWISS-2DPAGE; D4YYR7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000256|RuleBase:RU362042,
KW   ECO:0000313|EMBL:BAI95499.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM     38     57       Helical. {ECO:0000256|RuleBase:RU362042}.
FT   DOMAIN       57    144       Peptidase_S24. {ECO:0000259|Pfam:
FT                                PF00717}.
SQ   SEQUENCE   297 AA;  32524 MW;  DE4A06AECB22F743 CRC64;
     MTAADMTEND SASSDQPGSP ASEPEKTPVN WWQEVKSITL LILAVLAFHS FVAKPFYIPS
     ESMMPVLLKG DRLVVSKYPY GWSYVSPSFH PLPFLKGRIF GRLPERGDIV IVSPQNKRED
     YIKRVIGLPG DIVEVRGGQV VLNGVPVRQR VLKPIRIPVD GNAPCPPMQF PGALVTDASG
     RSWCELPVRQ EVLPNGKSYV TIDMGPSTLD WYGPVRVPAD HVFLMGDNRD NSADSRAPLE
     ENGLGGPVPW EAIGGRAEFI TFSLDGDSSW NPLSWLHAFR AGRAGNSLRP ASVTPPK
//

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