ID   FLGH_ECO24              Reviewed;         232 AA.
AC   A7ZKI4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=EcE24377A_1202;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(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; CP000800; ABV16813.1; -; Genomic_DNA.
DR   RefSeq; WP_001295442.1; NC_009801.1.
DR   AlphaFoldDB; A7ZKI4; -.
DR   SMR; A7ZKI4; -.
DR   EnsemblBacteria; ABV16813; ABV16813; EcE24377A_1202.
DR   GeneID; 66670654; -.
DR   KEGG; ecw:EcE24377A_1202; -.
DR   HOGENOM; CLU_069313_0_0_6; -.
DR   OMA; ITQQPMT; -.
DR   Proteomes; UP000001122; Chromosome.
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           22..232
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_1000060072"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   232 AA;  24615 MW;  862560170E6F63B7 CRC64;
     MQKNAAHTYA ISSLLVLSLT GCAWIPSTPL VQGATSAQPV PGPTPVANGS IFQSAQPINY
     GYQPLFEDRR PRNIGDTLTI VLQENVSASK SSSANASRDG KTNFGFDTVP RYLQGLFGNA
     RADVEASGGN TFNGKGGANA SNTFSGTLTV TVDQVLVNGN LHVVGEKQIA INQGTEFIRF
     SGVVNPRTIS GSNTVPSTQV ADARIEYVGN GYINEAQNMG WLQRFFLNLS PM