ID   FLGI_SHIDS              Reviewed;         365 AA.
AC   Q32EU0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, 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=SDY_2071;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR   EMBL; CP000034; ABB62165.1; -; Genomic_DNA.
DR   RefSeq; WP_005022057.1; NC_007606.1.
DR   RefSeq; YP_403656.1; NC_007606.1.
DR   AlphaFoldDB; Q32EU0; -.
DR   SMR; Q32EU0; -.
DR   STRING; 300267.SDY_2071; -.
DR   EnsemblBacteria; ABB62165; ABB62165; SDY_2071.
DR   KEGG; sdy:SDY_2071; -.
DR   PATRIC; fig|300267.13.peg.2487; -.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000002716; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           20..365
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000236319"
SQ   SEQUENCE   365 AA;  38214 MW;  D6DB3CDA7713F784 CRC64;
     MIKFLSALIL LLVTTAAQAE RIRDLTSVQG VRQNSLIGYG LVVGLDGTGD QTTQTPFTTQ
     TLNNMLSQLG ITVPTGTNMQ LKNVAAVMVT ASLPPFGRQG QTIDVVVSSM GNAKSLRGGT
     LLMTPLKGVD SQVYALAQGN ILVGGAGASA GGSSVQVNQL NGGRITNGAV IERELPSQFG
     VGNTLNLQLN DEDFSMAQQI ADTINRVRGY GSATVLDART IQVRVPSGNS SQVRFLADIQ
     NMQVNVTPQD AKVVINSRTG SVVMNREVTL DSCAVAQGNL SVTVNRQANV SQPDTPFGGG
     QTVVTPQTQI DLRQSGGSLQ SVRSSASLNN VVRSLNALGA TPMDLMSILQ SMQSAGCLRA
     KLEII