ID A0A0D1EBQ1_9RHOB Unreviewed; 239 AA.
AC A0A0D1EBQ1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Flagellar L-ring protein {ECO:0000256|HAMAP-Rule:MF_00415};
DE AltName: Full=Basal body L-ring protein {ECO:0000256|HAMAP-Rule:MF_00415};
GN Name=flgH {ECO:0000256|HAMAP-Rule:MF_00415,
GN ECO:0000313|EMBL:KIT14296.1};
GN ORFNames=jaqu_40900 {ECO:0000313|EMBL:KIT14296.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT14296.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT14296.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT14296.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
RL Submitted (FEB-2015) 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|HAMAP-Rule:MF_00415}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_00415}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00415}.
CC Bacterial flagellum basal body {ECO:0000256|HAMAP-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:KIT14296.1}.
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DR EMBL; JYFE01000081; KIT14296.1; -; Genomic_DNA.
DR RefSeq; WP_043920846.1; NZ_JYFE01000081.1.
DR AlphaFoldDB; A0A0D1EBQ1; -.
DR STRING; 935700.jaqu_40900; -.
DR PATRIC; fig|935700.4.peg.4216; -.
DR OrthoDB; 9789227at2; -.
DR Proteomes; UP000032232; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW Rule:MF_00415};
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_00415}; Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00415};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Reference proteome {ECO:0000313|Proteomes:UP000032232};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00415}.
SQ SEQUENCE 239 AA; 25464 MW; B5A11BA2B0E95153 CRC64;
MIRIVLIAAL AVGGCSRLQQ VGKAPDLTAV SGGNEHFAMT AGPALPATAE LRADDASLWE
AGRQSLLGDR RAGRRGDILT VVISIDERAE FANSSSRSRS GSESLSVTDL FGIPQRAADA
LPEGADLANA VDLNSSSDFG GDGAIRRKER LALRVAATVV EVLPNGVLRI EGTQEVRVNN
EVRVLLVTGF VRPEDVTRLN EITYDKIASA RISYGGRGQI TDVQQPRYGQ QVADILLPF
//
