FLAK_METMP
ID FLAK_METMP Reviewed; 230 AA.
AC Q6LZR9; Q8X252;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Preflagellin peptidase;
DE Short=PFP;
DE EC=3.4.23.52;
GN Name=flaK; OrderedLocusNames=MMP0555;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S2 / LL;
RA Leigh J.A.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=S2 / LL;
RX PubMed=11934494; DOI=10.1111/j.1574-6968.2002.tb11060.x;
RA Bardy S.L., Jarrell K.F.;
RT "FlaK of the archaeon Methanococcus maripaludis possesses preflagellin
RT peptidase activity.";
RL FEMS Microbiol. Lett. 208:53-59(2002).
CC -!- FUNCTION: Cleaves the N-terminal leader peptide from preflagellins.
CC {ECO:0000269|PubMed:11934494}.
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 Evidence={ECO:0000269|PubMed:11934494};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11934494};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11934494}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin
CC peptidase subfamily. {ECO:0000305}.
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; AF455758; AAL57886.1; -; Genomic_DNA.
DR EMBL; BX950229; CAF30111.1; -; Genomic_DNA.
DR RefSeq; WP_011170499.1; NC_005791.1.
DR AlphaFoldDB; Q6LZR9; -.
DR SMR; Q6LZR9; -.
DR STRING; 267377.MMP0555; -.
DR MEROPS; A24.016; -.
DR TCDB; 1.A.54.4.1; the presenilin er ca(2+) leak channel (presenilin) family.
DR EnsemblBacteria; CAF30111; CAF30111; MMP0555.
DR GeneID; 2761833; -.
DR KEGG; mmp:MMP0555; -.
DR PATRIC; fig|267377.15.peg.568; -.
DR eggNOG; arCOG02298; Archaea.
DR HOGENOM; CLU_1197648_0_0_2; -.
DR OMA; EEIWVTP; -.
DR OrthoDB; 87374at2157; -.
DR BioCyc; MMAR267377:MMP_RS02935-MON; -.
DR BRENDA; 3.4.23.52; 3262.
DR Proteomes; UP000000590; 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 1: Evidence at protein level;
KW Archaeal flagellum biogenesis; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Preflagellin peptidase"
FT /id="PRO_0000419279"
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..204
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 205..216
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 217..230
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 230 AA; 25915 MW; 2A2FCF99F0BD1D9F CRC64;
MIEYIIGVIG LLLASVQDFR SREIEDYIWI VLAVFGILFA IYSAITLSNY SILINSISGF
VICFILGYMM FLSGIGGGDG KILIGLGALV PKFQMPIYTS LGTLLNLNYI PNFPIMVFIN
GIFFMVFLPF VILFRNILNG ARPKTGKEVI LMFFGEKMKV KVAKEQKRLI MGQNDKINFF
PASDDEDFSK YGDEEEIWVT PQIPLIIPIT LSYLVTPIIG DRILDLLIPF
