ID   FLGH2_BURTA             Reviewed;         217 AA.
AC   Q2T8V7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Flagellar L-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH2 {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=BTH_II0190;
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_00415}.
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_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
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DR   EMBL; CP000085; ABC34266.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T8V7; -.
DR   SMR; Q2T8V7; -.
DR   PRIDE; Q2T8V7; -.
DR   DNASU; 3845136; -.
DR   EnsemblBacteria; ABC34266; ABC34266; BTH_II0190.
DR   KEGG; bte:BTH_II0190; -.
DR   HOGENOM; CLU_069313_0_2_4; -.
DR   OMA; QARISYG; -.
DR   Proteomes; UP000001930; Chromosome II.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           16..217
FT                   /note="Flagellar L-ring protein 2"
FT                   /id="PRO_0000236818"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   217 AA;  23275 MW;  87FB1222024F39C4 CRC64;
     MRILLALTWL AWLGACTSIE QPRPDFADDD LPPIATAPAA GRSGGVFNAV TAWSLASDGR
     AYRPGDTLTV TLEETTQASK RADTKFGKNG DMAVKPGVLF GSTVPFDSSF GAKRNFDGGG
     SSSQQNTLRG EITVIVNQVL AGGLLQVKGE KVLSLNQGEE VMRLSGYVRQ ADIDTNNRVS
     SRRIANARIK YVGKGALSDS NSAGWLTRFF NSPWMPF