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Database: UniProt
Entry: D9SJ61_GALCS
LinkDB: D9SJ61_GALCS
Original site: D9SJ61_GALCS 
ID   D9SJ61_GALCS            Unreviewed;       288 AA.
AC   D9SJ61;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-JAN-2019, entry version 42.
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=Galf_0292 {ECO:0000313|EMBL:ADL54337.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL54337.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL54337.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL54337.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E.,
RA   Emerson D., Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-2010) 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:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-
CC         terminal, basic peptide of 5-8 residues from type IV prepilin,
CC         and then N-methylates the new N-terminal amino group, the methyl
CC         donor being S-adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={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; CP002159; ADL54337.1; -; Genomic_DNA.
DR   RefSeq; WP_013292280.1; NC_014394.1.
DR   STRING; 395494.Galf_0292; -.
DR   MEROPS; A24.001; -.
DR   EnsemblBacteria; ADL54337; ADL54337; Galf_0292.
DR   KEGG; gca:Galf_0292; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248584; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; GCAP395494:G1GMJ-300-MONOMER; -.
DR   Proteomes; UP000001235; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001235};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ADL54337.1}; 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   Reference proteome {ECO:0000313|Proteomes:UP000001235};
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     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    260    278       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    125       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      135    244       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   288 AA;  31375 MW;  13462395AF9A080E CRC64;
     MTLFDLLESS APLFIGTCTL LGLMVGSFLN VVIHRLPKMM ELGWRSQCAE LRGEAPVESE
     PYNLLVPRSA CPQCQHAIRA WENIPVISYL LLRGKCSGCH TAISSRYPII ETFSGLLCGF
     AAFHFGFGLT ALAALILIWA LIALTAIDFD TQLLPDDITL PLLWAGLLFN LYGAFTSLHD
     AFLGAVFGYL ALWSVFWLFK LVTGKEGMGY GDFKLLAALG AWLGWQLLPL IIILSSLVGA
     IIGIALIIAV KRGREIPIPF GPYLAGGGLI ALFWGQTLTQ SYLQLLAP
//
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