ID   FLGH_CAMJJ              Reviewed;         232 AA.
AC   A1VZ42;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=CJJ81176_0710;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000538; EAQ72475.1; -; Genomic_DNA.
DR   RefSeq; WP_002861373.1; NC_008787.1.
DR   AlphaFoldDB; A1VZ42; -.
DR   SMR; A1VZ42; -.
DR   STRING; 354242.CJJ81176_0710; -.
DR   EnsemblBacteria; EAQ72475; EAQ72475; CJJ81176_0710.
DR   KEGG; cjj:CJJ81176_0710; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_1_7; -.
DR   OMA; ITQQPMT; -.
DR   Proteomes; UP000000646; 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..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           16..232
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_1000050086"
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   232 AA;  25168 MW;  05F7131228F0B4F0 CRC64;
     MKKVLFYVLP FAFFGCSATV DPQISMKPPA YVEELAPKQS NNVESAPGSL FGKGDNPLFS
     DKKAMNVNDL VTVVIQESTT QSTQANKATS RTNTSNLGGG ALTGSSGVVA NALNKVNAYS
     NIGFQTNSSN KYTGTGSQSR NESFNTTIST RVIKILSNGN YFIEGSRELL INGEKQIIQL
     SGVIRPYDIG QDNTIDSKYI ADAKILYKTE GEVDRSTRKP WGSKVIEAIW PF