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Database: UniProt
Entry: G2KPN6_MICAA
LinkDB: G2KPN6_MICAA
Original site: G2KPN6_MICAA 
ID   G2KPN6_MICAA            Unreviewed;       274 AA.
AC   G2KPN6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Prepilin leader peptidase/N-methyltransferase {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=MICA_1537 {ECO:0000313|EMBL:AEP09855.1};
OS   Micavibrio aeruginosavorus (strain ARL-13).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Micavibrio.
OX   NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09855.1, ECO:0000313|Proteomes:UP000009286};
RN   [1] {ECO:0000313|EMBL:AEP09855.1, ECO:0000313|Proteomes:UP000009286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09855.1,
RC   ECO:0000313|Proteomes:UP000009286};
RX   PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA   Wang Z., Kadouri D., Wu M.;
RT   "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT   aeruginosavorus ARL-13.";
RL   BMC Genomics 12:453-453(2011).
CC   -!- FUNCTION: Plays an essential role in type IV pili and type II
CC       pseudopili formation by proteolytically removing the leader sequence
CC       from substrate proteins and subsequently monomethylating the alpha-
CC       amino group of the newly exposed N-terminal phenylalanine.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-terminal,
CC         basic peptide of 5-8 residues from type IV prepilin, and then N-
CC         methylates the new N-terminal amino group, the methyl donor being S-
CC         adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={ECO:0000256|RuleBase:RU003794};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; CP002382; AEP09855.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2KPN6; -.
DR   STRING; 856793.MICA_1537; -.
DR   KEGG; mai:MICA_1537; -.
DR   eggNOG; COG1989; Bacteria.
DR   HOGENOM; CLU_057101_0_0_5; -.
DR   OMA; GAWGGWQ; -.
DR   OrthoDB; 9789291at2; -.
DR   Proteomes; UP000009286; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1220; -; 1.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   InterPro; IPR010627; Prepilin_pept_A24_N.
DR   PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE/N-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1.
DR   Pfam; PF06750; A24_N_bact; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000009286};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003794};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..103
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          116..225
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   274 AA;  29526 MW;  58AFEB3E52964F00 CRC64;
     MAGVDARTAL EILFVLMFGL CCGSFAAALI WRIPRGVSWI VAEKGAARSA CPHCQTPLTL
     WDLIPVFSWV FLRGRCRHCH APIGWIYPAI ELVSVILCLG VYALWGYSTL GGIVMLTVPF
     LVALFVIDLR HFILPDQLNA LVAFLGVVYQ FVLGGIVFAG TAIVSGVLWG VCAFGLGFLM
     KKILKKEALG FGDVKFFAVA GVWLPAVMAP PFLMWAGVMG VGLALIWKMA GRGAVFPFGP
     ALIVSFALCL ALTRVGLGLD LGQEQGLSFV RLSY
//
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