(data stored in SCRATCH zone)

SWISSPROT: A0LFU5_SYNFM

ID   A0LFU5_SYNFM            Unreviewed;       214 AA.
AC   A0LFU5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   OrderedLocusNames=Sfum_0598 {ECO:0000313|EMBL:ABK16297.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16297.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16297.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader
CC         sequences from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={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; CP000478; ABK16297.1; -; Genomic_DNA.
DR   RefSeq; WP_011697470.1; NC_008554.1.
DR   STRING; 335543.Sfum_0598; -.
DR   MEROPS; S26.025; -.
DR   EnsemblBacteria; ABK16297; ABK16297; Sfum_0598.
DR   KEGG; sfu:Sfum_0598; -.
DR   eggNOG; ENOG4105C3F; Bacteria.
DR   eggNOG; COG0681; LUCA.
DR   HOGENOM; HOG000003673; -.
DR   KO; K03100; -.
DR   OMA; NDSHIWG; -.
DR   OrthoDB; 1741894at2; -.
DR   BioCyc; SFUM335543:G1G7I-612-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; 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.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFU5.
DR   SWISS-2DPAGE; A0LFU5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Hydrolase {ECO:0000256|RuleBase:RU362042,
KW   ECO:0000313|EMBL:ABK16297.1};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN       45    127       Peptidase_S24. {ECO:0000259|Pfam:
FT                                PF00717}.
SQ   SEQUENCE   214 AA;  24921 MW;  76E247FD0DD94D2B CRC64;
     MTKTPIPTDR KPRPRQAVIW EYTRSILLGV VLALLIRTFI VQAYEIPSGS MEDTLAINDH
     ILVNKFIYGT KIPFTDLRIL EWREPARGDV VVFEYPLDPS KDYIKRIIGL PGDRIRIADR
     QVYINGQLYE NPHAIHKGRE IVPKLASPRD NTDPIVVPPN SYFVLGDNRD NSYDSRFWGF
     VRKDRIKGLA FIKYWAWDSE RHSVRWRSIG DVID
//

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