ID A0A1P8PZZ7_9LACO Unreviewed; 222 AA.
AC A0A1P8PZZ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:APX71194.1};
GN ORFNames=BTM29_00880 {ECO:0000313|EMBL:APX71194.1};
OS Companilactobacillus allii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1847728 {ECO:0000313|EMBL:APX71194.1, ECO:0000313|Proteomes:UP000187499};
RN [1] {ECO:0000313|Proteomes:UP000187499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WiKim39 {ECO:0000313|Proteomes:UP000187499};
RA Jung M.Y., Lee S.H.;
RL Submitted (DEC-2016) 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; CP019323; APX71194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8PZZ7; -.
DR STRING; 1847728.BTM29_00880; -.
DR KEGG; lalw:BTM29_00880; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000187499; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000187499};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..89
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 102..196
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 222 AA; 26037 MW; C951FB4D6188388B CRC64;
MTFLFYILVF VLSSSIVSFL TVVGYDFPKI EIMRRSKCNN CQKQLKWLEL FPVIGYLFLK
GRCRNCHKRI SWIYPTTELF GAIFVILAIY LEKNIYLFAP IFIMITLLAF MDFYHGFIYP
IFYLLSIPSF ILFIVFHHKI YLITGIITYL ILLCMYRFSK GIGMGDIEVL TILALFFGYT
SILNIILLAC IMCILHHLIN KKRSFRFIPY ITIATGIIFL IS
//
