(data stored in ACNUC7421 zone)

SWISSPROT: A8FQB3_SHESH

ID   A8FQB3_SHESH            Unreviewed;       303 AA.
AC   A8FQB3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU003794};
DE            EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794};
GN   OrderedLocusNames=Ssed_0423 {ECO:0000313|EMBL:ABV35036.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35036.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35036.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35036.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates
CC       the N-terminal (generally Phe) residue.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY: Typically cleaves a -Gly-|-Phe- bond to
CC       release an N-terminal, basic peptide of 5-8 residues from type IV
CC       prepilin, and then N-methylates the new N-terminal amino group,
CC       the methyl donor being S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; CP000821; ABV35036.1; -; Genomic_DNA.
DR   RefSeq; WP_012140773.1; NC_009831.1.
DR   STRING; 425104.Ssed_0423; -.
DR   MEROPS; A24.001; -.
DR   EnsemblBacteria; ABV35036; ABV35036; Ssed_0423.
DR   KEGG; sse:Ssed_0423; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248584; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; POG091H01KW; -.
DR   BioCyc; SSED425104:GH7Q-445-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010627; Pept_A24A_N.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   Pfam; PF06750; DiS_P_DiS; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
DR   PRODOM; A8FQB3.
DR   SWISS-2DPAGE; A8FQB3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ABV35036.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    166       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    175    192       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    198    220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    265       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    277    300       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    142       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      153    261       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   303 AA;  33706 MW;  CDCF3695E8F8CDE5 CRC64;
     MSEFISILSQ NLWLFSIISF IFSAVIGSFL NVVIHRFPVM LKREWQQECN QYLNEYHEKL
     IAPISEQLNN PIDDYPERYN LVVPASACPK CKTNIKPWHN LPIVGWLMLK GKCAACGTSI
     SPRYPIIELL TGLAVALLAY HFGPGWEFIF ATVLTFVLIA LTGIDLDEML LPDQLTLPLL
     WLGLLINLNG TFASPTDAMI GAAAGYLSLW SVFWAFKLLT GKEGMGYGDF KLLAVFGAWF
     GWQMLPLIIL LSSLVGAIVG IGLIVTKKIN KTNPIPFGPY IAAAGWIAMI WGSDITNWYL
     STL
//

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