ID   FLAK_HALMA              Reviewed;         341 AA.
AC   Q5UZH5;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Preflagellin peptidase;
DE            Short=PFP;
DE            EC=3.4.23.52;
GN   OrderedLocusNames=rrnAC2525;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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=AAV47328.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY596297; AAV47328.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049939013.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UZH5; -.
DR   STRING; 272569.rrnAC2525; -.
DR   EnsemblBacteria; AAV47328; AAV47328; rrnAC2525.
DR   GeneID; 40153419; -.
DR   KEGG; hma:rrnAC2525; -.
DR   PATRIC; fig|272569.17.peg.3133; -.
DR   eggNOG; arCOG02298; Archaea.
DR   HOGENOM; CLU_065732_0_0_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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..341
FT                   /note="Preflagellin peptidase"
FT                   /id="PRO_0000419276"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        25..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        53..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        87..92
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        104..126
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        156..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        325..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          219..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            24
FT                   /note="Essential for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            93
FT                   /note="Essential for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  36559 MW;  50DD6FB7691670EC CRC64;
     MLGSIPDLLR LVAVPVFGWA AYRDVKTRRV PNRTWTPLAA LAVVLLLWDA YTVWTGPTAV
     GQRLFLIRVA ISLGFVIPLS YGFWLIGGFG GADAKAFMLI AVLFPIYPVY YLPMPSVALP
     LQQTAIGVFS LTVLSNTVLA GVVYPLAVAA GNLARGRFSL AMFIGRPVAV PDVTEEYGRL
     LESPDGFDRG GLDLDALRMY LQWRGCSLAD IRADPAQRRL PTSLPAVPND PGDGSLATDG
     GDSASGDVAE PSANDIGADG MDHPDQIDDP WGAERFLDDI DHSAYGTSPQ QLRDGLDVLV
     EQDEVWISPG IPFLVPMFAG LVVSLTYGDV LFSLLQAVGL A