ID   FLGI2_BURTA             Reviewed;         369 AA.
AC   Q2T8V6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Flagellar P-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI2 {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=BTH_II0191;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC36282.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000085; ABC36282.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2T8V6; -.
DR   SMR; Q2T8V6; -.
DR   EnsemblBacteria; ABC36282; ABC36282; BTH_II0191.
DR   KEGG; bte:BTH_II0191; -.
DR   HOGENOM; CLU_045235_1_0_4; -.
DR   Proteomes; UP000001930; Chromosome II.
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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           25..369
FT                   /note="Flagellar P-ring protein 2"
FT                   /id="PRO_0000236297"
SQ   SEQUENCE   369 AA;  37801 MW;  BB900D1B859AE0FB CRC64;
     MCAFAAILSL LSVLLMATSR SSDAAPLGTL VSVEGVRDNQ LVGYGLVVGL NGSGDGQQIR
     YTGQSIANVL KQFGVTLPEG IRLRSRNVAA VMVSANFPAG YVPGQKIDVT VSSMGDAKSL
     RGGTLLLTPL RAADGVVYAL AQGNLVVPGV SAQGRSGSSV TINATAAGRI PQGATIEQEI
     PSDLDAKPSV RLSLKRPSFQ TATSIVAAID RMAGPGAATS RDGTSVEVRA PEDPTARVAF
     LAKLTAINVT PQKEPPRVVF NSRTGTVVIS QGMTVSPAAV SHGTLKVTIS EGAIVSQPNP
     LGGGKTAVVP LSQVDVQQDG NRMFNWPAGV SLQKIVDTIN STGASPDDVM AILQALDEAG
     ALNGELVVI