FLGI_SINMW
ID FLGI_SINMW Reviewed; 371 AA.
AC A6U639;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=Smed_0260;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR59119.1; -; Genomic_DNA.
DR RefSeq; WP_011974470.1; NC_009636.1.
DR RefSeq; YP_001325954.1; NC_009636.1.
DR AlphaFoldDB; A6U639; -.
DR SMR; A6U639; -.
DR STRING; 366394.Smed_0260; -.
DR EnsemblBacteria; ABR59119; ABR59119; Smed_0260.
DR GeneID; 61613100; -.
DR KEGG; smd:Smed_0260; -.
DR PATRIC; fig|366394.8.peg.3326; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_5; -.
DR OMA; KTIQITR; -.
DR OrthoDB; 693640at2; -.
DR Proteomes; UP000001108; Chromosome.
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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 26..371
FT /note="Flagellar P-ring protein"
FT /id="PRO_5000257212"
SQ SEQUENCE 371 AA; 38415 MW; 4AEDB18DCD91D7B4 CRC64;
MKMRACKWLL TLAVAFAATL SSAYAASRIK DVASLQAGRD NQLIGYGLVV GLQGTGDSLR
SSPFTDQSIR AMLQNLGIST QGGDSRTRNV AAVLVTATLP PFASPGSRLD VTVGSLGDAT
SLRGGTLVMT SLSGADGQIY AVAQGSVVVS GFNAQGEAAQ LNQGVTTAGR VPNGAIIERE
LPSKFKDGFN LVLQLRNPDF STAVGMAAAI NRYAAAQFGG RIAEALDSQS VLVQKPKMAD
LARLMADVEN LVIETDAPAR VVINERTGTI VIGQDVRVAQ VAVSYGTLTV QVSETPTIVQ
PEPFSRGQTA YEPNTTIEAQ SDGGTVAILN GSSLRSLVAG LNSIGVKPDG IIAILQSIKS
AGALQAELVL Q