ID   FLGI_BURMA              Reviewed;         389 AA.
AC   Q62ES6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, 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=BMA3332;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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=AAU48585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000010; AAU48585.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q62ES6; -.
DR   SMR; Q62ES6; -.
DR   STRING; 243160.BMA3332; -.
DR   EnsemblBacteria; AAU48585; AAU48585; BMA3332.
DR   KEGG; bma:BMA3332; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_4; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000006693; Chromosome 1.
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..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           34..389
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000041789"
SQ   SEQUENCE   389 AA;  39637 MW;  AB7711435EF27EB7 CRC64;
     MRPLVAARRR AAACCALAAC MLALAFAPAA ARAERLKDLA QIQGVRDNPL IGYGLVVGLD
     GTGDQTMQTP FTTQTLANML ANLGISINNG SANGGGSSAM TNMQLKNVAA VMVTATLPPF
     ARPGEAIDVT VSSLGNAKSL RGGTLLLTPL KGADGQVYAL AQGNMAVGGA GASANGSRVQ
     VNQLAAGRIA GGAIVERSVP NAVAQMNGVL QLQLNDMDYG TAQRIVSAVN SSFGAGTATA
     LDGRTIQLTA PADSAQQVAF MARLQNLEVS PERAAAKVIL NARTGSIVMN QMVTLQNCAV
     AHGNLSVVVN TQPVVSQPGP FSNGQTVVAQ QSQIQLKQDN GSLRMVTAGA NLAEVVKALN
     SLGATPADLM SILQAMKAAG ALRADLEII