ID   FLGI_BORPA              Reviewed;         368 AA.
AC   Q7WA91;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 69.
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=BPP1492;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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: 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   -!- SEQUENCE CAUTION:
CC       Sequence=CAE36794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX640427; CAE36794.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7WA91; -.
DR   SMR; Q7WA91; -.
DR   EnsemblBacteria; CAE36794; CAE36794; BPP1492.
DR   KEGG; bpa:BPP1492; -.
DR   HOGENOM; CLU_045235_1_0_4; -.
DR   Proteomes; UP000001421; 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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           23..368
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000041785"
SQ   SEQUENCE   368 AA;  38145 MW;  5D385A3B9302EB4D CRC64;
     MLIPLARAVL ALALLGAGAA HAERLKDLAS IQGVRGNQLI GYGLVVGLDG SGDQVRQTPF
     TQQSLTNMLS QLGITVPQGS NMQLKNVAAV MVTATLPSFA RPGQTVDVVV SSMGNAKSLR
     GGTLLMTPLK GADNQVYAIA QGNLLVGGAG ASAGGSSVQI NQLNGGRISN GAIVERAVPT
     MYAQDGTVYL EMNNTDFGTT QNAAAAINRQ FGAGTAMALD GRVIQVRGPL DPSMMPAFMS
     QVENLQVARA PATAKVIINA RTGSVVMNRT VMIEEAAVAH GNLSVIINRQ NQVFQPDTPF
     TEGQTVVVPN TQIEVRQDGG ALQRVTTSAN LADVVKALNA LGATPQDLLA ILQAMKTAGA
     LRADLEII