ID   FLGI_WIGBR              Reviewed;         370 AA.
AC   Q8D3F6;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=WIGBR0450;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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: Bacterial flagellum basal body
CC       {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; BA000021; BAC24191.1; -; Genomic_DNA.
DR   RefSeq; WP_011069849.1; NC_004344.2.
DR   AlphaFoldDB; Q8D3F6; -.
DR   SMR; Q8D3F6; -.
DR   STRING; 36870.25166000; -.
DR   EnsemblBacteria; BAC24191; BAC24191; BAC24191.
DR   KEGG; wbr:flgI; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000562; 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; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           22..370
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009530"
SQ   SEQUENCE   370 AA;  39548 MW;  E8323F2FE212B7C5 CRC64;
     MKYILIKLSI VMIFIINSAS KAERIRDLTT IVGVRDNVLI GYGLVVGLDG TGDQTTQTPF
     TIQSLRNMLS QLGVSIPSGI NMQLKNIAAV MVTAKLPPFV KIGQKIDVMV SSLGSAKSLR
     GGTLLITPLK GVDNQIYALA QGNILVSGFG AQSGGNTSQV NQLNGGRISE GAIIEKSIKT
     DFDKREIITL QLNNNDFSLA QQISDAINTY FGKKSAYPTD SRTINVILSA SYDKSEKVKF
     IARLQNIPII IGPSDAIIVI NSRTGSVVIN KEVMLNSCAV AHGELTVEIK KRTKVNQPNT
     ILGGGSTVVT PETEILIKNQ GDSLQEISSS TNLNEVISSL NSIGAKPNDL MAILESMKSA
     GCLNAKLEIN