FLAK_METM6
ID FLAK_METM6 Reviewed; 230 AA.
AC A9A677;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Preflagellin peptidase;
DE Short=PFP;
DE EC=3.4.23.52;
GN Name=flaK; OrderedLocusNames=MmarC6_0338;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-23; GLU-25; ASP-26; GLY-76;
RP GLY-77; GLY-78 AND PRO-208.
RC STRAIN=C6 / ATCC BAA-1332;
RX PubMed=21765428; DOI=10.1038/nature10218;
RA Hu J., Xue Y., Lee S., Ha Y.;
RT "The crystal structure of GXGD membrane protease FlaK.";
RL Nature 475:528-531(2011).
CC -!- FUNCTION: Cleaves the N-terminal leader peptide from preflagellins.
CC {ECO:0000269|PubMed:21765428}.
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:21765428};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21765428};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21765428}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin
CC peptidase subfamily. {ECO:0000305}.
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DR EMBL; CP000867; ABX01159.1; -; Genomic_DNA.
DR RefSeq; WP_012193134.1; NC_009975.1.
DR PDB; 3S0X; X-ray; 3.60 A; A/B=1-230.
DR PDBsum; 3S0X; -.
DR AlphaFoldDB; A9A677; -.
DR SMR; A9A677; -.
DR STRING; 444158.MmarC6_0338; -.
DR MEROPS; A24.016; -.
DR EnsemblBacteria; ABX01159; ABX01159; MmarC6_0338.
DR GeneID; 5739084; -.
DR KEGG; mmx:MmarC6_0338; -.
DR eggNOG; arCOG02298; Archaea.
DR HOGENOM; CLU_1197648_0_0_2; -.
DR OMA; EEIWVTP; -.
DR OrthoDB; 87374at2157; -.
DR BRENDA; 3.4.23.52; 3262.
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 3D-structure; Archaeal flagellum biogenesis; Cell membrane; Hydrolase;
KW Membrane; Protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Preflagellin peptidase"
FT /id="PRO_0000419277"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2..18
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 19..23
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 47..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 73..78
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 79..89
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 90..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..139
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 140..204
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..216
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 217..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 18
FT /note="Essential for catalysis"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Essential for catalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="E->A: No effect on proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 25
FT /note="E->A: No effect on proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 26
FT /note="D->A: No effect on proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 76
FT /note="G->A: Large reduction in proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 77
FT /note="G->A: No effect on proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 78
FT /note="G->A: No effect on proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
FT MUTAGEN 208
FT /note="P->A: Enhanced proteolytic activity."
FT /evidence="ECO:0000269|PubMed:21765428"
SQ SEQUENCE 230 AA; 26021 MW; 879C0EE8E214E61A CRC64;
MIEYIIGALG LIIASVQDFR SREIEDYIWI FLAVFGVLFA IYSSITLLDY SILINSISGF
VICFILGYMM FLSGIGGGDG KMLIGLGALV PKFQMPIYTS LGTLLNLNYV PTFPIMVFIN
GIFFMVFLPF VILFRNILNG ARPKTGKEFI LMFFGEKMKV NVAKEQKRLI MGQNDKINFF
PAADDEDFSK YSNNEEIWVT PQIPLIIPIT LSYLVTPIIG DRILDFLIPF
