ID   FLAK_METJA              Reviewed;         234 AA.
AC   Q58312;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Preflagellin peptidase;
DE            Short=PFP;
DE            EC=3.4.23.52;
GN   Name=flaK; OrderedLocusNames=MJ0902;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Cleaves the N-terminal leader peptide from preflagellins.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves the signal peptide of 3 to 12 amino acids from the N-
CC         terminal of preflagellin, usually at Arg-Gly-|- or Lys-Gly-|-, to
CC         release flagellin.; EC=3.4.23.52;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin
CC       peptidase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98907.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98907.1; ALT_INIT; Genomic_DNA.
DR   PIR; F64412; F64412.
DR   RefSeq; WP_064496655.1; NC_000909.1.
DR   AlphaFoldDB; Q58312; -.
DR   SMR; Q58312; -.
DR   STRING; 243232.MJ_0902; -.
DR   MEROPS; A24.016; -.
DR   EnsemblBacteria; AAB98907; AAB98907; MJ_0902.
DR   GeneID; 1451791; -.
DR   KEGG; mja:MJ_0902; -.
DR   eggNOG; arCOG02298; Archaea.
DR   HOGENOM; CLU_1197648_0_0_2; -.
DR   InParanoid; Q58312; -.
DR   OrthoDB; 87374at2157; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR009655; Preflagellin_peptidase_C.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   Pfam; PF06847; Arc_PepC_II; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
PE   3: Inferred from homology;
KW   Archaeal flagellum biogenesis; Cell membrane; Hydrolase; Membrane;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..234
FT                   /note="Preflagellin peptidase"
FT                   /id="PRO_0000107094"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        2..18
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        19..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        47..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        50..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        73..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        79..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        90..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        111..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        140..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        206..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        218..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Essential for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Essential for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  26294 MW;  A0F94DDCA7F7D2D4 CRC64;
     MINFIVGAIG LLIASIYDLK SREIEDYVWV SMVIFGLIYN GYLSFISHDM LYVIQSIVGF
     IVCFFLGFFM FLLGVGGGDG KLIMGLGALI PKYNMPIHTP LGAILNYLYL PSFPIMVVIN
     AMFFSITLPI IIFLRNVIRG VKPKTKKEVL CMFLGEKMKV SEAIKKERLI LGNHENLKLL
     PSAEKDCDFS KFDKNEEIWV TPAIPFVVPI FLSYLLTSII GDKIIGIFLS VFGL