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Database: UniProt
Entry: U6C0B5_9BACT
LinkDB: U6C0B5_9BACT
Original site: U6C0B5_9BACT 
ID   U6C0B5_9BACT            Unreviewed;       224 AA.
AC   U6C0B5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-FEB-2023, entry version 32.
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};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:BAO02570.1};
RN   [1] {ECO:0000313|EMBL:BAO02570.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24098725;
RA   Uchiyama T., Miyazaki K.;
RT   "Metagenomic screening for aromatic compound-responsive transcriptional
RT   regulators.";
RL   PLoS ONE 8:e75795-e75795(2013).
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}.
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DR   EMBL; AB828163; BAO02570.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6C0B5; -.
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}; Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Cell projection {ECO:0000313|EMBL:BAO02570.1};
KW   Cilium {ECO:0000313|EMBL:BAO02570.1};
KW   Flagellum {ECO:0000313|EMBL:BAO02570.1};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00415}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..224
FT                   /note="Flagellar L-ring protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008976549"
SQ   SEQUENCE   224 AA;  24033 MW;  E0B69E0637E4309D CRC64;
     MSRYCTLVFM VLLSGCVVQQ TEVMSPSFDQ QLKPPVQTYS NGSIWQASSI ALTEDGKARR
     IGDIVTIIVT ETASASKEAA TATGRSSSLS AGIPNMLGLE GSKIITSNFA DLSNLINASA
     SSSFDGSGST SRKETLTATI SAKVIDVLAN GNMKIEGRRN VKVNSEDQIV TVRGTVRQRD
     ISPENTINSS YIADAQITYS GEGIISDRQQ PGWLMNVIDK LWPF
//
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