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FLGH_BRUA2
ID   FLGH_BRUA2              Reviewed;         238 AA.
AC   Q2YJ67;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Flagellar L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=BAB2_0156;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00415}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00415}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00415}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00415}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ12322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM040265; CAJ12322.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2YJ67; -.
DR   SMR; Q2YJ67; -.
DR   STRING; 359391.BAB2_0156; -.
DR   EnsemblBacteria; CAJ12322; CAJ12322; BAB2_0156.
DR   KEGG; bmf:BAB2_0156; -.
DR   HOGENOM; CLU_069313_1_2_5; -.
DR   Proteomes; UP000002719; Chromosome II.
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; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           17..238
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000236815"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   238 AA;  25471 MW;  98DBC6109CE9896D CRC64;
     MNKAILAVAM VLLLAGCATK PEEIGRAPDL SPVAAHLGMQ NNPQFNGYPA RPGKASYSLW
     DQRSTNFFKD PRAATPGDVL TVIISINDRA NLDNKTDRER VSKGIYGGGG SFATSSITGA
     AAGGDMDASV NTHSDSKSKG KGTIERSEDI RLQIAAIVTD TLPNGNLIIR GSQEVRVNNE
     LRVLNVAGVV RPRDISGNNT ISYDKIAEAR ISYGGRGRLS EIQQPPYGQQ ILDQFSPF
 
 
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