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Database: UniProt
Entry: N9MQ38_9GAMM
LinkDB: N9MQ38_9GAMM
Original site: N9MQ38_9GAMM 
ID   N9MQ38_9GAMM            Unreviewed;       286 AA.
AC   N9MQ38;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   13-FEB-2019, entry version 24.
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=F897_00869 {ECO:0000313|EMBL:ENX10674.1};
OS   Acinetobacter variabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX10674.1, ECO:0000313|Proteomes:UP000013101};
RN   [1] {ECO:0000313|EMBL:ENX10674.1, ECO:0000313|Proteomes:UP000013101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX10674.1,
RC   ECO:0000313|Proteomes:UP000013101};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. NIPH 2171.";
RL   Submitted (FEB-2013) 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}.
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:ENX10674.1}.
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DR   EMBL; APRS01000006; ENX10674.1; -; Genomic_DNA.
DR   RefSeq; WP_005233531.1; NZ_KB850112.1.
DR   EnsemblBacteria; ENX10674; ENX10674; F897_00869.
DR   PATRIC; fig|1217693.3.peg.836; -.
DR   Proteomes; UP000013101; Unassembled WGS sequence.
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:UP000013101};
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     14     35       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    116    149       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    161    178       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    276       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    127       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      138    247       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   286 AA;  32109 MW;  E81907C24E4CAB0F CRC64;
     MQDFILYFSQ NPTALYLAVG LFSLCIGSFL NVVIYRTPKM MEQEWRTDCQ LFLHPDQPII
     DESKITLSKP ASTCPKCQTP IRWYQNIPVI SWILLRGKCG NCQNPISIRY PFIELLTAAC
     ALIVVAVFGP TIQMLFGLVF TYVLIALTFI DFDTQLLPDR YTLPLAALGL GINSYAIYTT
     PNSAIWGYII GFLCLWVVYY LFKLVTGKEG MGYGDFKLLA ALGAWMGPML LPLIVLLSSL
     VGAIIGIILL KVRKENQPFA FGPYIAIAGW IAFLWGEQIM KIYLGQ
//
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