FLGH_BURCJ
ID FLGH_BURCJ Reviewed; 229 AA.
AC B4E8L3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE Flags: Precursor;
GN Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415};
GN OrderedLocusNames=BceJ2315_05670; ORFNames=BCAL0570;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR50880.1; -; Genomic_DNA.
DR RefSeq; WP_006495504.1; NC_011000.1.
DR AlphaFoldDB; B4E8L3; -.
DR SMR; B4E8L3; -.
DR STRING; 216591.BCAL0570; -.
DR EnsemblBacteria; CAR50880; CAR50880; BCAL0570.
DR GeneID; 56559614; -.
DR KEGG; bcj:BCAL0570; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_0_4; -.
DR OMA; ITQQPMT; -.
DR OrthoDB; 1900876at2; -.
DR BioCyc; BCEN216591:G1G1V-646-MON; -.
DR Proteomes; UP000001035; Chromosome 1.
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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 26..229
FT /note="Flagellar L-ring protein"
FT /id="PRO_1000123941"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ SEQUENCE 229 AA; 24102 MW; 95EF86FE3D5C3C03 CRC64;
MKQVRLPSSA TVRAACAVAV AALAGCAQIP RDPIIQQPMT AQPPMPMSMQ APGSIYNPGF
AGRPLFEDQR PRNIGDILTI MIAENINATK SSGANTNRQG NTDFNVPTAG FLGGLFAKAN
LSATGANKFA ATGGASAANT FNGTITVTVT NVLPNGNLVV SGEKQMLINQ GNEFVRFSGV
VNPNTISGAN SVYSTQVADA KIEYSSKGYI NEAETMGWLQ RFFLNIAPW