ID K0CJ17_ALCDB Unreviewed; 227 AA.
AC K0CJ17;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:AFT71697.1};
GN OrderedLocusNames=B5T_03430 {ECO:0000313|EMBL:AFT71697.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71697.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71697.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000256|ARBA:ARBA00006929,
CC ECO:0000256|HAMAP-Rule:MF_00415}.
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DR EMBL; CP003466; AFT71697.1; -; Genomic_DNA.
DR AlphaFoldDB; K0CJ17; -.
DR STRING; 930169.B5T_03430; -.
DR KEGG; adi:B5T_03430; -.
DR PATRIC; fig|930169.3.peg.3390; -.
DR eggNOG; COG2063; Bacteria.
DR HOGENOM; CLU_069313_0_0_6; -.
DR OMA; WLARFFL; -.
DR Proteomes; UP000006286; 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; FLAGELLAR L-RING PROTEIN; 1.
DR PANTHER; PTHR34933:SF3; 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:AFT71697.1};
KW Cilium {ECO:0000313|EMBL:AFT71697.1};
KW Flagellum {ECO:0000313|EMBL:AFT71697.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 227 AA; 24525 MW; 6CCF3B4D292A1FF6 CRC64;
MPGSPSSDPR LWGLALGLSL LAGCAQLPRP SVVGEQERVE IAQPPAPQAN GSIFQARRGY
HPLFEDNRPR MAGDVLTIVF DEEVSASKVS SSNANRTGNS TFTPQVLPKG LEDLADYGFD
LSGANTFESG GGSRANNSFT GTLTVTVLEV LRNGNLRVRG EKQIAINQGT EFIRFAGVVD
PQVIRGDNSV LSTRVADARI EYVGDGYINE AQHMGWLQRF FLNISPF
//