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Database: UniProt
Entry: A0A1Z4K4Q5_9CYAN
LinkDB: A0A1Z4K4Q5_9CYAN
Original site: A0A1Z4K4Q5_9CYAN 
ID   A0A1Z4K4Q5_9CYAN        Unreviewed;       273 AA.
AC   A0A1Z4K4Q5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   05-DEC-2018, entry version 6.
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=NIES22_40720 {ECO:0000313|EMBL:BAY63982.1};
OS   Calothrix brevissima NIES-22.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=1973478 {ECO:0000313|EMBL:BAY63982.1, ECO:0000313|Proteomes:UP000218201};
RN   [1] {ECO:0000313|EMBL:BAY63982.1, ECO:0000313|Proteomes:UP000218201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-22 {ECO:0000313|EMBL:BAY63982.1,
RC   ECO:0000313|Proteomes:UP000218201};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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; AP018207; BAY63982.1; -; Genomic_DNA.
DR   Proteomes; UP000218201; 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:UP000218201};
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   Reference proteome {ECO:0000313|Proteomes:UP000218201};
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     28       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     85    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    149       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    161    187       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    207    232       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    244    266       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       16     97       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      109    227       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   273 AA;  29289 MW;  76B4829170DDCE7D CRC64;
     MDILIILPAS AVVFALGASI GSFINVVVYR LPAGLSVLWP PSRCPHCLNQ LKAYDNVPVF
     GWLWLKGRCR YCKSKISARY PVVEALTGVI FLLVFLLFKV SILTIGYWAF CSWLLALSLI
     DLDTMTLPNQ LTQSGLVLGI IFQIVIGLFP EGSSVGAIRH LMMGIVGAVV GLWLFDAIAL
     FGSIALGKTA MGAGDAKLAA MMGAWLGWKY LLLAAFIACG VGTLVGIASI TFSKHRFGQK
     IPFGPFLAIG AAIALFGGEA ILSAYLRLFF PVI
//
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