ID M6FE51_9LEPT Unreviewed; 283 AA.
AC M6FE51;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase, A24 type IV prepilin peptidase family protein {ECO:0000313|EMBL:EMK25362.1};
GN ORFNames=LEP1GSC008_1818 {ECO:0000313|EMBL:EMK25362.1};
OS Leptospira kirschneri serovar Bulgarica str. Nikolaevo.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1240687 {ECO:0000313|EMBL:EMK25362.1, ECO:0000313|Proteomes:UP000011980};
RN [1] {ECO:0000313|EMBL:EMK25362.1, ECO:0000313|Proteomes:UP000011980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nikolaevo {ECO:0000313|EMBL:EMK25362.1,
RC ECO:0000313|Proteomes:UP000011980};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-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:EMK25362.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANCE01000061; EMK25362.1; -; Genomic_DNA.
DR RefSeq; WP_020762843.1; NZ_ANCE01000061.1.
DR AlphaFoldDB; M6FE51; -.
DR PATRIC; fig|1240687.3.peg.967; -.
DR OrthoDB; 345277at2; -.
DR Proteomes; UP000011980; 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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..115
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 127..232
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 283 AA; 32523 MW; 9C48CD5083AAB894 CRC64;
MLISPDSFSF WIILCFGSLG AASLGSFYVT LGFRILETYY GKVRKLFSPF EKWKYILTRP
SSCDHCGKKI RYPELFPIIG FFISKGICKY CNKKIYVLFP LVEFLFVCIF VFCFIITKNV
PFSFTFLFLC GHLLISCLTD AFHFSLDYEN LPWILCFGVA SIFLLDGKLP SLNDLFVLGG
FFVTFLILFF FFPGGIGFGD VLFAPVYAFL AGHPWWMFFL NASYIPAVLF TIILRERGKS
IRKTPIPMGL YFGIGLFFTF LSRVFFESDL APFTLFSEYS NPD
//
