ID A0A0S8DI99_9BACT Unreviewed; 238 AA.
AC A0A0S8DI99;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 20.
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 ORFNames=AMK70_04415 {ECO:0000313|EMBL:KPK35896.1};
OS Nitrospira bacterium SG8_35_1.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK35896.1, ECO:0000313|Proteomes:UP000052010};
RN [1] {ECO:0000313|EMBL:KPK35896.1, ECO:0000313|Proteomes:UP000052010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK35896.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}. 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:KPK35896.1}.
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DR EMBL; LJTK01000055; KPK35896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DI99; -.
DR Proteomes; UP000052010; 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 Membrane {ECO:0000256|HAMAP-Rule:MF_00415};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..238
FT /note="Flagellar L-ring protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008856287"
SQ SEQUENCE 238 AA; 26169 MW; 4D65B2D2F375D9ED CRC64;
MCTVQLVCSG ISVLMLVASC ASPSAKLPLP PPKYVYHTPE VEETKSANSL WRDSSNLFED
RKARRVNDLV TINIVESLSG SGTADTDTKR ESTAEYDMTK FFGMNTDFNL QNAWLLKNMY
KGANIFEPVV QGSGQSEFKG SGDTNREGSL DATITAKVVE VMPNGNLVLE SRKELTINNE
KQILVLSGVV RPDDISANNS IDSNLIADAK IYYVGDGVIQ DKQSPGWLVR VLDHLWAF
//
