ID M7S506_HELPX Unreviewed; 237 AA.
AC M7S506;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Flagellar L-ring protein {ECO:0000256|ARBA:ARBA00016940, ECO:0000256|HAMAP-Rule:MF_00415};
DE AltName: Full=Basal body L-ring protein {ECO:0000256|ARBA:ARBA00032876, ECO:0000256|HAMAP-Rule:MF_00415};
GN Name=flgH {ECO:0000256|HAMAP-Rule:MF_00415};
GN ORFNames=HPHPH1_0389 {ECO:0000313|EMBL:EMR59303.1};
OS Helicobacter pylori Hp H-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992058 {ECO:0000313|EMBL:EMR59303.1, ECO:0000313|Proteomes:UP000011947};
RN [1] {ECO:0000313|EMBL:EMR59303.1, ECO:0000313|Proteomes:UP000011947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-1 {ECO:0000313|EMBL:EMR59303.1,
RC ECO:0000313|Proteomes:UP000011947};
RA Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT "Comparitive Sequence Analysis of H. pylori Isolates.";
RL Submitted (FEB-2013) 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:0000256|ARBA:ARBA00002591, ECO:0000256|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:0000256|ARBA:ARBA00011439, ECO:0000256|HAMAP-
CC Rule:MF_00415}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_00415}. Bacterial flagellum basal body {ECO:0000256|HAMAP-
CC Rule:MF_00415}.
CC -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000256|ARBA:ARBA00006929,
CC ECO:0000256|HAMAP-Rule:MF_00415}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR59303.1}.
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DR EMBL; AOTX01000009; EMR59303.1; -; Genomic_DNA.
DR RefSeq; WP_000709968.1; NZ_AOTX01000009.1.
DR AlphaFoldDB; M7S506; -.
DR PATRIC; fig|992058.3.peg.406; -.
DR Proteomes; UP000011947; Unassembled WGS sequence.
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; FLAGELLAR L-RING PROTEIN; 1.
DR PANTHER; PTHR34933:SF1; FLAGELLAR L-RING PROTEIN; 1.
DR Pfam; PF02107; FlgH; 1.
DR PRINTS; PR01008; FLGLRINGFLGH.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_00415}; Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Cell projection {ECO:0000313|EMBL:EMR59303.1};
KW Cilium {ECO:0000313|EMBL:EMR59303.1};
KW Flagellum {ECO:0000313|EMBL:EMR59303.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..237
FT /note="Flagellar L-ring protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004084529"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 26425 MW; 9996704494263BB3 CRC64;
MKKALYLGAV AFGVAFSMAS ANEPNIDFNP PNYVEETPSK EFIPELNKLG SLFGQGERPL
FADRRAMKPN DLITIIVSEK ASANYSSSKD YKSASGGNST PPRLTYNGLD ERKKKEAEYL
DDKNNYNFTK SSNNTNFKGG GSQKKSEDLE IVLSARIIKV LENGNYFIYG NKEVLVDGEK
QILKVSGVIR PYDIERNNTI QSKFLADAKI EYTNLGHLSD SNKKKFAADA METQMPY
//
