FLGH_VIBC3
ID FLGH_VIBC3 Reviewed; 261 AA.
AC A5F678; C3M3F1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=VC0395_A1786, VC395_2310;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21250.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10300.1; -; Genomic_DNA.
DR RefSeq; WP_000729679.1; NZ_CP045719.1.
DR AlphaFoldDB; A5F678; -.
DR SMR; A5F678; -.
DR STRING; 345073.VC395_2310; -.
DR EnsemblBacteria; ABQ21250; ABQ21250; VC0395_A1786.
DR KEGG; vco:VC0395_A1786; -.
DR KEGG; vcr:VC395_2310; -.
DR PATRIC; fig|345073.21.peg.2226; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_2_6; -.
DR OMA; ITQQPMT; -.
DR Proteomes; UP000000249; Chromosome 2.
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..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 19..261
FT /note="Flagellar L-ring protein"
FT /id="PRO_1000123962"
FT REGION 37..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ SEQUENCE 261 AA; 27790 MW; 585B3E01F1C6396B CRC64;
MAAMKRLLAS SLLILLSGCS LMQPPIESAE TIQGTTTVDA VEGDKSESNS GLTDALRNRT
DPVAGDPAWA PIHPKGKPEH YAAETGSLFN LASSSSMYDD SKPRGVGDII TVTLNESTKA
AKSADADLNK KNDASMDPLA VGGKDLTIGD YNFSYALKND NKFSGSAAAN QSNSMSGSIT
VEVIEVLANG NLVIRGEKWL TLNTGDEYIR LSGTIRPDDI DFDNTIASNR ISNARIQYSG
TGTNQDMQEP GFLARFFNVS L