FLIN_PECCC
ID FLIN_PECCC Reviewed; 106 AA.
AC P35539;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Flagellar motor switch protein FliN;
DE AltName: Full=Flagellar motor switch protein MopA;
DE Flags: Fragment;
GN Name=fliN; Synonyms=mopA;
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).
CC -!- FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form
CC the rotor-mounted switch complex (C ring), located at the base of the
CC basal body. This complex interacts with the CheY and CheZ chemotaxis
CC proteins, in addition to contacting components of the motor that
CC determine the direction of flagellar rotation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Bacterial flagellum basal body {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family. {ECO:0000305}.
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DR EMBL; X72969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S35274; S35274.
DR AlphaFoldDB; P35539; -.
DR SMR; P35539; -.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.330.10; -; 1.
DR InterPro; IPR012826; FliN.
DR InterPro; IPR001543; FliN-like_C.
DR InterPro; IPR001172; FliN_T3SS_HrcQb.
DR InterPro; IPR036429; SpoA-like_sf.
DR Pfam; PF01052; FliMN_C; 1.
DR PRINTS; PR00956; FLGMOTORFLIN.
DR SUPFAM; SSF101801; SSF101801; 1.
DR TIGRFAMs; TIGR02480; fliN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Chemotaxis;
KW Flagellar rotation; Membrane.
FT CHAIN <1..106
FT /note="Flagellar motor switch protein FliN"
FT /id="PRO_0000184120"
FT NON_TER 1
SQ SEQUENCE 106 AA; 11623 MW; 3E377D8A24FD2F75 CRC64;
RPTTEGIFKS LDGHDPLGAL QDIDLILDIP VKLTVELGRT KMTIKELLRL TQGSVVALDG
LAGEPLDILI NGYLIAQGEV VVVSDKYGVR ITDIITPSER MRRLSR