ID Q7UFL4_RHOBA Unreviewed; 457 AA.
AC Q7UFL4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Prepilin peptidase, type IV {ECO:0000313|EMBL:CAD78668.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:CAD78668.1};
DE EC=3.4.99.- {ECO:0000313|EMBL:CAD78668.1};
GN OrderedLocusNames=RB8494 {ECO:0000313|EMBL:CAD78668.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD78668.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD78668.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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DR EMBL; BX294147; CAD78668.1; -; Genomic_DNA.
DR RefSeq; NP_868390.1; NC_005027.1.
DR AlphaFoldDB; Q7UFL4; -.
DR STRING; 243090.RB8494; -.
DR EnsemblBacteria; CAD78668; CAD78668; RB8494.
DR KEGG; rba:RB8494; -.
DR PATRIC; fig|243090.15.peg.4082; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_598361_0_0_0; -.
DR InParanoid; Q7UFL4; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAD78668.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:CAD78668.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Transferase {ECO:0000313|EMBL:CAD78668.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..154
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT REGION 415..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 50073 MW; C0F252939DDD0254 CRC64;
MASRVCGHAK GHAILSRRRS PYRILAVCLL IGYLLASAAY VWLSALWISG AHPHFRVVDL
LMPRANDVVI FTFFLVVGAS VGSFLNVVVW RLPQRLNVNG HSFCPRCRNR LRARDNVPIF
GWLWLSGRCR DCRLPISSRY PIVETLVGIT FALVGATELT RWSLPYFGDS VRPNWMWTPI
VDADLLTLIL YHVVALATAW AMGLIRFDGK ALPSRLTLFA AVTLIGGMFA FPQAMVVPWQ
LVGESMPAGI GTWPPSGWMT TGAEWSVTLV QIGLRLLTSL VAAGFFARVL AKSFCPSADM
KMDPLGSSTK RLIDLMILIA VPAIVVGWQA VMGVILLAAV FAKILGMCEF AQSRDSLGRF
AVSLPVATSV QLLLWRGLVA SQVWPSEQAS QVGLIVSFFG VLTIPLWLDE NGESFPPMGD
ESGNGGVSDH FDEDVREAQA SRKDPDALQQ GDSFELN
//
