ID   FLGI_BUCAP              Reviewed;         369 AA.
AC   Q8K9K2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   25-MAY-2022, entry version 92.
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=BUsg_332;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM67886.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE013218; AAM67886.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8K9K2; -.
DR   SMR; Q8K9K2; -.
DR   STRING; 198804.BUsg_332; -.
DR   EnsemblBacteria; AAM67886; AAM67886; BUsg_332.
DR   KEGG; bas:BUsg_332; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000000416; 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; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           25..369
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009496"
SQ   SEQUENCE   369 AA;  40615 MW;  349E5502BFCE6A3E CRC64;
     MSKTISLLKF IICILISLCS FTYAEKIRDL TSIEGIRDNQ LIGYGLIVGL DGTGDQSTQT
     PFTNQSLHNM LSQLGVTIPP DTNMHLKNVA AVIVTANLPP FSHTGEAIDV VVSSMGDAKS
     LKGGTLLMTP LRGADNQIYA IAQGNILVSE KNNLKKNNSI FSNQVNSGRI NHGATIEREI
     NTDFGKKKII NLQLNKEDFG IAQKISDMIN VQYPDTATAL NSKTVQLNTY ANNTIQVHML
     SNIQNIDISM PSQEAKVIIN PRTGSIVINQ EVKLGTCIVS HGDLSILIEK KEEEKINSFL
     FETLRKNQKE SFLKNIINRN YINNNSVKNT SLNNIVRVLN SLGTKPNELI SILQLMKNAG
     CLHAKLEIV