GenomeNet

Database: UniProt
Entry: A0A1W9NYA8_9BACT
LinkDB: A0A1W9NYA8_9BACT
Original site: A0A1W9NYA8_9BACT 
ID   A0A1W9NYA8_9BACT        Unreviewed;       381 AA.
AC   A0A1W9NYA8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   10-APR-2019, entry version 7.
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=B5M53_12425 {ECO:0000313|EMBL:OQX50503.1};
OS   Candidatus Cloacimonas sp. 4484_209.
OC   Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas.
OX   NCBI_TaxID=1968525 {ECO:0000313|EMBL:OQX50503.1};
RN   [1] {ECO:0000313|EMBL:OQX50503.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4484_209 {ECO:0000313|EMBL:OQX50503.1};
RX   PubMed=28835260; DOI=10.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial
RT   hydrocarbon and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
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:OQX50503.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; MZGI01000265; OQX50503.1; -; 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; IPR005495; LptG/LptF_permease.
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; PF03739; LptF_LptG; 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      6     24       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     94    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    166       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    178    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    220    243       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    255    280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    306    326       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8     90       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      102    201       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   381 AA;  43095 MW;  099E7FE0A44DD155 CRC64;
     MNEVFVFISG LVVGSFLNVC IYRIPRNESL LYPPSHCPFC GAHIRWSDNI PIISYIILKG
     RCRNCGAHIP IRYPLVEFLS ATILILLYER FSLSLLFLKY AVFSYALLTI TFIDIKHLIV
     PDRIVLPLIL LGILFSLPHH VLKSIVGIAG GFVLFVLIAI IGKILFKKEA LGGGDIKLIA
     ACGAFLGITG VIITTFLSAF FRKMVLVDKY IIKQLTKTFF SSFIILTALM LFAGVIQISH
     IVFVQGITVK ILLKIFYQQA TFVAIFTIPM ALTVAVNFVY VDFAKNNEII AFQTSGISKL
     NIYKPAFYFT IFIFLISFLN VSSIAYKQRG EFHLTLLQLT RHKIYSEISE RSFFRFSKGS
     VIYAETISPD TFFLWLLLAW V
//
DBGET integrated database retrieval system