ID   FLGI_BUCBP              Reviewed;         375 AA.
AC   Q89AH5;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-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=bbp_315;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27037.1; -; Genomic_DNA.
DR   RefSeq; WP_011091438.1; NC_004545.1.
DR   AlphaFoldDB; Q89AH5; -.
DR   SMR; Q89AH5; -.
DR   STRING; 224915.bbp_315; -.
DR   EnsemblBacteria; AAO27037; AAO27037; bbp_315.
DR   GeneID; 56470854; -.
DR   KEGG; bab:bbp_315; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; QFRPKNV; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000601; 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..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           24..375
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009497"
SQ   SEQUENCE   375 AA;  42130 MW;  261C6A1AD7E7610A CRC64;
     MFNQSFLKYM LFGFFLFSFH AHADRIRDLI TIQGIRYNQL IGYGLVVGLD GTGDRTNQIS
     YTTHALKNML FQLGITFPNE QNAKFKNIAA VMVTTKFPNF THIGQQVDVI VSSVGDATSL
     QGGTLLMTPL RGTDNKIYAV AQGNIIINDK NSVERFKNIL VNNHLNNGMI INGATIEREM
     HTDFGKNETL NLQLNNEDFT VAQEISKKIN MQYPKSAVAL NSKIIQVCIP NNNIEQVEML
     ATIQNINIPI PIQDAKILIN AKTGNIITNQ TININTCAIT HKNISMTIAF NKLKINRLVP
     NPIIKSDKNN NKTLNDEQIY KNNYNTNNFQ YLEKTSNLNT IICALNLFDI TTTELISILQ
     SMHDAGCFHA KLEIT