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Database: UniProt
Entry: FLGH2_YERPS
LinkDB: FLGH2_YERPS
Original site: FLGH2_YERPS 
ID   FLGH2_YERPS             Reviewed;         221 AA.
AC   Q666C4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Flagellar L-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00415};
DE   AltName: Full=Basal body L-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00415};
DE   Flags: Precursor;
GN   Name=flgH2 {ECO:0000255|HAMAP-Rule:MF_00415}; OrderedLocusNames=YPTB3334;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
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DR   EMBL; BX936398; CAH22572.1; -; Genomic_DNA.
DR   RefSeq; WP_011193059.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q666C4; -.
DR   SMR; Q666C4; -.
DR   GeneID; 66844244; -.
DR   KEGG; yps:YPTB3334; -.
DR   Proteomes; UP000001011; 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: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; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           17..221
FT                   /note="Flagellar L-ring protein 2"
FT                   /id="PRO_0000009490"
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   221 AA;  24025 MW;  7D3F8DA3C3E30859 CRC64;
     MKRFLILTPM VLALCGCESP ALLVQKDDAE FAPPANLVQP ATVTEGGGLF QPAYNWSLLQ
     DRRAYRIGDI LTVILDESTQ SSKQAKTNFG KKNDMSLGVP EVLGKKLNKF GGSISGKRDF
     DGSATSAQQN MLRGSITVAV HQVLPNGVLV IRGEKWLTLN QGDEYMRVTG LVRADDVARD
     NSVSSQRIAN ARISYAGRGA LSDANSAGWL TRFFNHPLFP I
//
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