ID A0A0Q9Y2F4_9STAP Unreviewed; 234 AA.
AC A0A0Q9Y2F4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Signal peptidase {ECO:0000313|EMBL:KRG10369.1};
GN ORFNames=ACA31_05680 {ECO:0000313|EMBL:KRG10369.1};
OS Staphylococcus sp. NAM3COL9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1667172 {ECO:0000313|EMBL:KRG10369.1, ECO:0000313|Proteomes:UP000051126};
RN [1] {ECO:0000313|EMBL:KRG10369.1, ECO:0000313|Proteomes:UP000051126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA309 {ECO:0000313|EMBL:KRG10369.1,
RC ECO:0000313|Proteomes:UP000051126};
RA Gaiero J., Nicol R., Habash M.;
RT "Genome sequencing project of Staphylococcus sp. NA309.";
RL Submitted (JUN-2015) 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:KRG10369.1}.
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DR EMBL; LGPC01000011; KRG10369.1; -; Genomic_DNA.
DR RefSeq; WP_057512382.1; NZ_LGPC01000011.1.
DR AlphaFoldDB; A0A0Q9Y2F4; -.
DR PATRIC; fig|1667172.3.peg.1170; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000051126; 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 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..85
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 98..194
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 234 AA; 27102 MW; 0C21E5AE5215CB4C CRC64;
MIKQLLLCPV LFSYLYQLSY VNQLKLNYFV LRSRCDYCHR GLKFTEMIPI ISFLCLKGRS
SCCQSKLSSL YLIGEFLSIA PAFVLSYLSI PLDQATFLLI YIFLLVFTMY DIKTFALPLP
LYIIFSLCSY FITQGNVYHC IIMTTVLHFF YFLVRHGIGY GDILLFSLLS YLLPYPYFVL
TMLFTFICGG VFALVSMIFF RNIKQKTPLI PFIFVAFNLT IISHQYLTLG VGLI
//