FLIR_PECCC
ID FLIR_PECCC Reviewed; 261 AA.
AC P34202;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Flagellar biosynthetic protein FliR;
DE AltName: Full=Flagellar biosynthetic protein MopE;
GN Name=fliR; Synonyms=mopE;
OS Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SCRI 193;
RX PubMed=8412685; DOI=10.1111/j.1365-2958.1993.tb01695.x;
RA Mulholland V., Hinton J.C.D., Sidebotham J., Toth I.K., Hyman L.J.,
RA Perombelon M.C.M., Reeves P.J., Salmond G.P.C.;
RT "A pleiotropic reduced virulence (Rvi-) mutant of Erwinia carotovora
RT subspecies atroseptica is defective in flagella assembly proteins that are
RT conserved in plant and animal bacterial pathogens.";
RL Mol. Microbiol. 9:343-356(1993).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=7934865; DOI=10.1111/j.1365-2958.1993.tb00986.x;
RA Mulholland V., Hinton J.C.D., Sidebotham J., Toth I.K., Hyman L.J.,
RA Perombelon M.C.M., Reeves P.J., Salmond G.P.C.;
RT "A pleiotropic reduced virulence (Rvi-) mutant of Erwinia carotovora
RT subspecies atroseptica is defective in flagella assembly proteins that are
RT conserved in plant and animal bacterial pathogens.";
RL Mol. Microbiol. 10:1154-1154(1993).
CC -!- FUNCTION: Role in flagellar biosynthesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Bacterial flagellum basal body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FliR/MopE/SpaR family. {ECO:0000305}.
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DR EMBL; X72969; CAA51478.1; -; Genomic_DNA.
DR PIR; S42698; S42698.
DR AlphaFoldDB; P34202; -.
DR SMR; P34202; -.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
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:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR InterPro; IPR006303; FliR.
DR InterPro; IPR002010; T3SS_IM_R.
DR PANTHER; PTHR30065; PTHR30065; 1.
DR Pfam; PF01311; Bac_export_1; 1.
DR PRINTS; PR00953; TYPE3IMRPROT.
DR TIGRFAMs; TIGR01400; fliR; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..261
FT /note="Flagellar biosynthetic protein FliR"
FT /id="PRO_0000192057"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 28399 MW; A9EAC26238A76654 CRC64;
MLTFNSWDMV NWVSQFFWPF VRILALISTA PVFNERAIGN RVKIGLGVLI TLLVAPYLPL
NTTPIFSVAG VWLLIQQILI GVTLGLSMQL AFAAIRHAGE LIGLQMGLAF ATFFDPTGGP
NMQVVARFLN ILAILLFLTF DGHLWMISLL ADSFYTLPIS ANPIISHAFL ALARAGGLIF
INGLMLALPI ITLLLTINLA LGMLNRVAPQ LSIFVVGFPI TLTVGIMTLG LLLPLIPPFA
EHLFSEVFDL LADILTQLSS S