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Database: UniProt
Entry: FLGI_SINFN
LinkDB: FLGI_SINFN
Original site: FLGI_SINFN 
ID   FLGI_SINFN              Reviewed;         371 AA.
AC   C3MG26;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=NGR_c02790;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24077.1; -; Genomic_DNA.
DR   RefSeq; WP_012706862.1; NC_012587.1.
DR   RefSeq; YP_002824830.1; NC_012587.1.
DR   AlphaFoldDB; C3MG26; -.
DR   SMR; C3MG26; -.
DR   STRING; 394.NGR_c02790; -.
DR   KEGG; rhi:NGR_c02790; -.
DR   PATRIC; fig|394.7.peg.3080; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_5; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000001054; 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; FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI; 1.
DR   PANTHER; PTHR30381:SF0; FLAGELLAR P-RING PROTEIN; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Periplasm; Reference proteome; 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_1000134841"
SQ   SEQUENCE   371 AA;  38362 MW;  FA3C7375C530052C CRC64;
     MTMRVCKWLL TFALLFAATL TPAHSASRIK DVASLQAGRD NQLIGYGLVV GLQGTGDSLR
     SSPFTDQSIR AMLQNLGIST QGGESRTRNV AAVLVTATLP PFASPGSRVD VTVGSLGDAT
     SLRGGTLVMT SLSGADGQIY AVAQGSIVVT GFSAQGDAAS LSQGVTTAGR VPNGAIIERE
     LPSKFKDGFN LVLQLRNPDF STAVGMAAAI NKFASAQFGG RIAEALDSQS VLVQKPKMAD
     LARLMADIEN LVVETDVPAR VVVNERTGTI VIGQDVRVNE VAVSYGTLTV QVTETPTVVQ
     PAPFSRGETA VEPNTTIEAQ SDGGTVAILN GSSLRSLVAG LNSIGVKPDG IIAILQSIKT
     AGALQAELVL Q
//
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