FLGI_LEGPA
ID FLGI_LEGPA Reviewed; 367 AA.
AC Q5X5T9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Flagellar P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=lpp1231;
OS Legionella pneumophila (strain Paris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Paris;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
CC -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC protects the motor/basal body from shearing forces during rotation.
CC {ECO:0000255|HAMAP-Rule:MF_00416}.
CC -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC organelle and consists of four rings (L,P,S, and M) mounted on a
CC central rod. {ECO:0000255|HAMAP-Rule:MF_00416}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC Rule:MF_00416}.
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DR EMBL; CR628336; CAH12382.1; -; Genomic_DNA.
DR RefSeq; WP_011213581.1; NC_006368.1.
DR AlphaFoldDB; Q5X5T9; -.
DR SMR; Q5X5T9; -.
DR KEGG; lpp:lpp1231; -.
DR LegioList; lpp1231; -.
DR HOGENOM; CLU_045235_1_0_6; -.
DR OMA; KTIQITR; -.
DR GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR HAMAP; MF_00416; FlgI; 1.
DR InterPro; IPR001782; Flag_FlgI.
DR PANTHER; PTHR30381; PTHR30381; 1.
DR Pfam; PF02119; FlgI; 1.
DR PRINTS; PR01010; FLGPRINGFLGI.
PE 3: Inferred from homology;
KW Bacterial flagellum; Periplasm; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 23..367
FT /note="Flagellar P-ring protein"
FT /id="PRO_0000041797"
SQ SEQUENCE 367 AA; 38425 MW; A12ED392E01304E7 CRC64;
MRRILVIRWI LAIHLIATQV FAERIKDIAT LAGVRVNQLV GYGLVVGLSG TGDKTGTKFT
EDSFANMLTQ LGINIPPGVR LNSKNIAAVM VTANLSSFMK KGQTMDVNIS SIGDSKSLLG
GTLLLTPLKG ADGRVYAMSQ GNIVVSGISA SGSDGSSVTV NVPSGGRIPN GATIEADIPN
PFYYSNSLTY NLHTPDFTTA KRMSDAINEL MGPGTAKAID AGSVVVTAPK KLSQRVDYVS
VLENIEFKPG EPMAKIIINA RTGTVVISSN VIVKSAAVSH GNLVVSITET PVISQPNAFA
SGRTVATQQS QVNIQQKNNR AFILPKGTTL KDIVRGINAV GATPADVISI LEALQQAGAL
SATLIVI