FLGH_ALIF1
ID FLGH_ALIF1 Reviewed; 263 AA.
AC Q5E3N0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
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}; OrderedLocusNames=VF_1871;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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; CP000020; AAW86366.1; -; Genomic_DNA.
DR RefSeq; WP_011262373.1; NC_006840.2.
DR RefSeq; YP_205254.1; NC_006840.2.
DR AlphaFoldDB; Q5E3N0; -.
DR SMR; Q5E3N0; -.
DR STRING; 312309.VF_1871; -.
DR EnsemblBacteria; AAW86366; AAW86366; VF_1871.
DR GeneID; 64242028; -.
DR KEGG; vfi:VF_1871; -.
DR PATRIC; fig|312309.11.peg.1898; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_2_6; -.
DR OMA; ITQQPMT; -.
DR OrthoDB; 1900876at2; -.
DR Proteomes; UP000000537; Chromosome I.
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 Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT CHAIN 16..263
FT /note="Flagellar L-ring protein"
FT /id="PRO_0000009477"
FT REGION 123..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 263 AA; 28555 MW; 13246FE804B5A593 CRC64;
MKRLLCLLLL TTLTGCETLL IKNPSAQESE VTSATTNVDA VEGDKAKEED SGIIDTLRGR
NDPIAGDPAW APIHPKEKPE HYAAATGSLF NVDHAQDMYD DTKPRGLGDI VTVMLAENTK
AAKSADAELS KSNDSSMDPL QVGGQELQMG GQYNFSYELS NDNNFTGNTS ANQSNSLSGS
ITVEVIEVLS NGNLLIRGEK WLTLNTGDEY IRLSGTIRPD DINFDNTIDS TRISNARIQY
SGTGDQQDMQ EPGFLARFFN VAL
