ID E8X4M4_GRATM Unreviewed; 314 AA.
AC E8X4M4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Prepilin peptidase {ECO:0000313|EMBL:ADW69434.1};
DE EC=3.4.23.43 {ECO:0000313|EMBL:ADW69434.1};
GN OrderedLocusNames=AciX9_2397 {ECO:0000313|EMBL:ADW69434.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000256|ARBA:ARBA00005801}.
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DR EMBL; CP002480; ADW69434.1; -; Genomic_DNA.
DR RefSeq; WP_013580750.1; NC_015064.1.
DR AlphaFoldDB; E8X4M4; -.
DR STRING; 1198114.AciX9_2397; -.
DR PaxDb; 1198114-AciX9_2397; -.
DR KEGG; acm:AciX9_2397; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_1_0; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000000343; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.120.1220; -; 1.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:ADW69434.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..91
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 127..271
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 314 AA; 34349 MW; FDE7F1C00CB0EECA CRC64;
MLSPVFFEAA GLLLGLLFGS FLNVCISRLP QHQSVVTPRS KCPGCEHPIR WFDNIPLLSW
VLLRGRCRDC KERISWRYPA VELATGLWFA RAGAQIRELH YVSAFGLGPL SGSQLLEGYV
QILAIAVLGF LLIGLIVMDW QTQRLPDAFT LGGIFAGLFL VCTQAIFLGP TEAQINLTSH
HLRMSSPGSF VGRGNVFLTG PEHLIFGRLL AVAGIAAILL TIRALYKAVR HRDGLGLGDV
KMLAMVAAFL GFWPTILTLF LGTFLASAYA IPLVLRRRAN ALTKLPFGSF LGIAGLLAAL
FAEPILNWYA GLFR
//
