ID   FLGI_BORA1              Reviewed;         376 AA.
AC   Q2L1B1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=BAV1695;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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}.
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; AM167904; CAJ49303.1; -; Genomic_DNA.
DR   RefSeq; WP_012417364.1; NC_010645.1.
DR   AlphaFoldDB; Q2L1B1; -.
DR   SMR; Q2L1B1; -.
DR   STRING; 360910.BAV1695; -.
DR   EnsemblBacteria; CAJ49303; CAJ49303; BAV1695.
DR   GeneID; 41393546; -.
DR   KEGG; bav:BAV1695; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_4; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000001977; 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; Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           30..376
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000236296"
SQ   SEQUENCE   376 AA;  39028 MW;  0EFDF00AA3624C71 CRC64;
     MTQRPFSLLS HLGRICLAAA MLAALPAQAA ERLKDLATFQ GVRGNQLIGY GLVVGLDGTG
     DQVRQTPFTQ QSLTNMLSQL GITVPAGSNM QLKNVAAVMV TATLPAFARP GQTVDVVVSS
     MGNAKSLRGG TLLMTPLKGA DNSVYAIAQG NVLVGGAGAS AGGSSVQINT LNGGRISAGA
     IVERPVPTSF AQDGLVYLEM NNSDFGTTQN AANAINRQFG AGTAMVMDAR VLQLRGPLDP
     SQMPAFLSQI ENLPVTLAPA VAKVIINART GSVVMNRTVT IEEAAVAHGN LSVIINRQNQ
     VFQPDTPFTD GQTVVAPNTQ IEVRQEGGAL QRVRTSANLA DVVKALNALG ATPQDLLAIL
     QAMKAAGALR AELEII