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Database: UniProt
Entry: K0CJ17_ALCDB
LinkDB: K0CJ17_ALCDB
Original site: K0CJ17_ALCDB 
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
//
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