ID A0A1F5ZSX3_9BACT Unreviewed; 255 AA.
AC A0A1F5ZSX3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Prepilin peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3D77_02720 {ECO:0000313|EMBL:OGG15586.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_39_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798382 {ECO:0000313|EMBL:OGG15586.1, ECO:0000313|Proteomes:UP000176923};
RN [1] {ECO:0000313|EMBL:OGG15586.1, ECO:0000313|Proteomes:UP000176923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG15586.1}.
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DR EMBL; MFJL01000022; OGG15586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5ZSX3; -.
DR STRING; 1798382.A3D77_02720; -.
DR Proteomes; UP000176923; 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 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 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 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..90
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 106..210
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 255 AA; 28509 MW; BB57535036713ED8 CRC64;
MELILPAIIL GSCIGSFLNV VIDRLSSGKS IVTPQSHCDK CKRFLTPLEL IPVLSYIYLK
GRCKTCHTKL SIQYPLSEIV TGLIFGYLMW FVINTGLSFV YWIYLCIIFS CLIVVIGTDL
KKRIILDEIV FFGTVVSFLY ILFFDPASLL SHIFSAFVFL GFFLFLFLIT KGKGMGFGDV
KFSFFMGLTL GYPQIIVGFY LAFLTGALVS LILVIGRVKS FKSTVPFGPY LALAMGISLL
FGDVLWQTAL RVLNL
//
