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Database: UniProt
Entry: A0A1F6B1P5_9BACT
LinkDB: A0A1F6B1P5_9BACT
Original site: A0A1F6B1P5_9BACT 
ID   A0A1F6B1P5_9BACT        Unreviewed;       248 AA.
AC   A0A1F6B1P5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 5.
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   ORFNames=A2973_03050 {ECO:0000313|EMBL:OGG30723.1};
OS   Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_49_10.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1798396 {ECO:0000313|EMBL:OGG30723.1};
RN   [1] {ECO:0000313|EMBL:OGG30723.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OGG30723.1}.
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DR   EMBL; MFJZ01000006; OGG30723.1; -; Genomic_DNA.
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   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   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     91    112       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    119    138       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    144    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    177    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    247       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8     90       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      101    205       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   248 AA;  27359 MW;  A0C3DEEA164E2C97 CRC64;
     MDRIVAFLFG TIVGSFLSVL SDRLPRHEQV VWGRSYCDHC KKLLRWYELV PIASYLVQGG
     RCRRCKGKLS FQYPVVECMT GIGFVLITQK FLPPLVSLCV MVLFCSLLVI TVSDMKYKII
     PDSMVVSGIV AAGFLLLINN SSTYALYFVS ALGAAAFFLI LWMATRGCGM GLGDVKLAFL
     LGLWLGFPYI VIALYLAFLT GATTGVILIL AQKKTLKSRI PFGPFMILGA ATAAIWSTQA
     GILWRIFL
//
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