ID   FLGH_BARBK              Reviewed;         230 AA.
AC   A1UTU3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BARBAKC583_1137;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
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; CP000524; ABM45595.1; -; Genomic_DNA.
DR   RefSeq; WP_005767762.1; NC_008783.1.
DR   AlphaFoldDB; A1UTU3; -.
DR   SMR; A1UTU3; -.
DR   STRING; 360095.BARBAKC583_1137; -.
DR   EnsemblBacteria; ABM45595; ABM45595; BARBAKC583_1137.
DR   KEGG; bbk:BARBAKC583_1137; -.
DR   PATRIC; fig|360095.6.peg.1098; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_1_2_5; -.
DR   OMA; ITQQPMT; -.
DR   OrthoDB; 1900876at2; -.
DR   Proteomes; UP000000643; 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.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           17..230
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_1000050080"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   230 AA;  25439 MW;  1C1685F6CC0CF01D CRC64;
     MYLVFGIIFT SVIVTSCSYN TKDFNSVPDF SPVRADLGYA PSRTAQTYPL PPRESNYSLY
     RASGNSFFRD PRAMQPGDVL TVQISINDRA SLNNKSDLKS DSSSKYTIGT GYSFMDRIAG
     SLEGESSNQS KGDGKIERQE NIRLSVAAIV TDVLPNGNLI IRGSQEVRVN HELRILNIAG
     VVRPRDISGN NMIEYDKIAE ARISYGGRGR ISEIQQPPYG QQLLNQISPF