FLAK_METVO
ID FLAK_METVO Reviewed; 233 AA.
AC Q8NKW5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Preflagellin peptidase;
DE Short=PFP;
DE EC=3.4.23.52;
GN Name=flaK;
OS Methanococcus voltae.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2188;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RA Feldman R., Overbeek R., Whitman W.B.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10633127; DOI=10.1128/jb.182.3.855-858.2000;
RA Correia J.D., Jarrell K.F.;
RT "Posttranslational processing of Methanococcus voltae preflagellin by
RT preflagellin peptidases of M. voltae and other methanogens.";
RL J. Bacteriol. 182:855-858(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TOPOLOGY, AND
RP MUTAGENESIS OF ASP-18; ASP-79; ASP-186; ASP-190 AND ASP-224.
RX PubMed=14622420; DOI=10.1046/j.1365-2958.2003.03758.x;
RA Bardy S.L., Jarrell K.F.;
RT "Cleavage of preflagellins by an aspartic acid signal peptidase is
RT essential for flagellation in the archaeon Methanococcus voltae.";
RL Mol. Microbiol. 50:1339-1347(2003).
CC -!- FUNCTION: Cleaves the N-terminal leader peptide from preflagellins. The
CC processing of preflagellins is necessary for assembly of flagellins
CC into a flagellum structure. {ECO:0000269|PubMed:10633127,
CC ECO:0000269|PubMed:14622420}.
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:10633127, ECO:0000269|PubMed:14622420};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:10633127};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:10633127};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10633127};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10633127}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are non-motile and non-
CC flagellated. The flagellins of the mutant have larger molecular weights
CC than their wild-type counterparts, as expected if they retain their
CC 11- to 12-amino-acid leader peptide. {ECO:0000269|PubMed:14622420}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family. Archaeal preflagellin
CC peptidase subfamily. {ECO:0000305}.
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DR EMBL; AF508194; AAM34242.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NKW5; -.
DR SMR; Q8NKW5; -.
DR MEROPS; A24.016; -.
DR BioCyc; MetaCyc:MON-16809; -.
DR BRENDA; 3.4.23.52; 3268.
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; IPR000045; Prepilin_IV_endopep_pep.
DR Pfam; PF01478; Peptidase_A24; 1.
PE 1: Evidence at protein level;
KW Archaeal flagellum biogenesis; Cell membrane; Hydrolase; Membrane;
KW Protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..233
FT /note="Preflagellin peptidase"
FT /id="PRO_0000419278"
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..207
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..219
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 220..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT SITE 18
FT /note="Essential for catalysis"
FT SITE 79
FT /note="Essential for catalysis"
FT MUTAGEN 18
FT /note="D->A,N: Loss of preflagellin peptidase activity."
FT /evidence="ECO:0000269|PubMed:14622420"
FT MUTAGEN 79
FT /note="D->A,N: Loss of preflagellin peptidase activity."
FT /evidence="ECO:0000269|PubMed:14622420"
FT MUTAGEN 79
FT /note="D->E: Still able to process preflagellin to mature
FT flagellin."
FT /evidence="ECO:0000269|PubMed:14622420"
FT MUTAGEN 186
FT /note="D->A: Still able to process preflagellin to mature
FT flagellin."
FT /evidence="ECO:0000269|PubMed:14622420"
FT MUTAGEN 190
FT /note="D->A: Still able to process preflagellin to mature
FT flagellin."
FT /evidence="ECO:0000269|PubMed:14622420"
FT MUTAGEN 224
FT /note="D->A: Still able to process preflagellin to mature
FT flagellin."
FT /evidence="ECO:0000269|PubMed:14622420"
SQ SEQUENCE 233 AA; 25888 MW; 3C1BE743D40B5309 CRC64;
MIAYAIGLLG LLIASIQDIK SREIENYIWI GMAVIGLLLS TYLSFTTGNF MPIISSISGF
IICFIIGYLM FVLGIGGADG KILMGMGALI PSYAFPVYSS LQPLYTMEYI PWFPLLVFFN
GVILMIVLPI YLFFKNLSNG VKPKKLKEYV LMLVGEYITV AEAKKGNKVV LGKGKDVKLI
PSVNDDKNYD LSKYKDTQYV WATPELPLLV PIALSYIITP FLGDKILSII LPM
