ID R3J2H8_ENTFL Unreviewed; 230 AA.
AC R3J2H8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Type III leader peptidase {ECO:0000313|EMBL:EOJ95579.1};
GN ORFNames=WOK_03247 {ECO:0000313|EMBL:EOJ95579.1};
OS Enterococcus faecalis EnGen0359.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1169307 {ECO:0000313|EMBL:EOJ95579.1, ECO:0000313|Proteomes:UP000013601};
RN [1] {ECO:0000313|EMBL:EOJ95579.1, ECO:0000313|Proteomes:UP000013601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR197 {ECO:0000313|EMBL:EOJ95579.1,
RC ECO:0000313|Proteomes:UP000013601};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus faecalis TR197.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOJ95579.1}.
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DR EMBL; ASDV01000016; EOJ95579.1; -; Genomic_DNA.
DR RefSeq; WP_010826814.1; NZ_KB944820.1.
DR AlphaFoldDB; R3J2H8; -.
DR PATRIC; fig|1169307.3.peg.3242; -.
DR HOGENOM; CLU_057101_1_1_9; -.
DR Proteomes; UP000013601; Unassembled WGS sequence.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..88
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 99..200
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 230 AA; 26217 MW; 54A72D5ED33DBC95 CRC64;
MFFLSLFLIG ACFGSFLCLV AERLPVGRSL WWPPSHCQGC HQPLQLYELI PVVSILLQRF
RCRKCQQPVA KSYLLAELVM GSLTASCFSA GLTIDALILW WWLTSAFTLS LIDYWYLVVE
PKILYPSFFV LCLLKMAGQH SFYLLTGLFC FCFFRAVLYY FPEAMGRGDL LLLGLWGCFL
QVPQLLMLLF FASSYGLIYG YSCKFLGYPV EQTLPFVPFL SLGLLTISCL
//