FRZF_MYXXA
ID FRZF_MYXXA Reviewed; 593 AA.
AC P31759;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein methyltransferase FrzF;
DE EC=2.1.1.80;
GN Name=frzF;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DZF1;
RX PubMed=2168368; DOI=10.1128/jb.172.9.4877-4887.1990;
RA McCleary W.R., McBride M.J., Zusman D.R.;
RT "Developmental sensory transduction in Myxococcus xanthus involves
RT methylation and demethylation of FrzCD.";
RL J. Bacteriol. 172:4877-4887(1990).
CC -!- FUNCTION: This methyltransferase is one of the proteins required for
CC the normal aggregation of M.xanthus cells during fruiting body
CC formation. It is also a component of a sensory transduction pathway
CC that controls the frequency at which cells reverse their gliding
CC direction. It may methylate FrzCD to form gamma-glutamyl methyl ester
CC residues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
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DR EMBL; M35200; AAA25398.1; -; Genomic_DNA.
DR PIR; B36707; XYYZFG.
DR RefSeq; WP_011554141.1; NZ_FNOH01000003.1.
DR AlphaFoldDB; P31759; -.
DR SMR; P31759; -.
DR GeneID; 41361457; -.
DR OMA; PLCVEAR; -.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.155.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF01739; CheR; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Chemotaxis; Methyltransferase; Repeat; S-adenosyl-L-methionine; TPR repeat;
KW Transferase.
FT CHAIN 1..593
FT /note="Protein methyltransferase FrzF"
FT /id="PRO_0000176046"
FT DOMAIN 1..276
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT REPEAT 423..456
FT /note="TPR 1"
FT REPEAT 457..490
FT /note="TPR 2"
FT REPEAT 491..524
FT /note="TPR 3"
SQ SEQUENCE 593 AA; 64669 MW; B38BA5F481A082B9 CRC64;
MLTASQKVLQ QLAALLLERA GLKITPDGFH SLRLALSARM PVLGLEEPEH YIQRLTGAGG
EEELRSLLPL VTVGHTEFFR DAKQFRALEK SVLPDLVSRS RREMRKVSIW SAGCATGEEP
YSLAMVLAEL GALSLEVDLW ATDLNLAAVE AAKQGRFTSR RAISINQARL TRFFKPVEEG
YEALPALREY IRFDGQNLAV PVFDKVALSS LDLILCRNVI IYFDLPTIRG LMDRFLAALR
PGGLLFLGYS ESLFKVYDRF EMIEVDGAFV YRRPLNDKSM RAPPLRITPY PGEPDVAARR
PVPADAFTAD LRKRMLPEDV PLTTRLPAVS ASSVAAPGSP SVTLPALGAS SSPRSVVPGR
LPAVSPHSPL PAIAARSRVT AELPTVGSVD SARPRITTEL PAVATTPRAP TVEVPAWPTL
LPPAERLAMA VRKMAQGDFS AAIAGVQRLL ADEPSDLDGL LTLGNLFSLT GRIPEAREAF
AQAIQREPLC VEARVFGGVA ALQAGELSEA RSELSKALFL EPTLAIGHYL LAQVHERTQD
HEAARRSYRN AIAQLRFPQR PLAGHYPEMP DSADAISRAA RYALAALEEQ PLR