ID   FLGH2_VIBPA             Reviewed;         223 AA.
AC   Q87JI3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=VPA0270;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC61613.1; -; Genomic_DNA.
DR   RefSeq; NP_799780.1; NC_004605.1.
DR   RefSeq; WP_011106240.1; NC_004605.1.
DR   AlphaFoldDB; Q87JI3; -.
DR   SMR; Q87JI3; -.
DR   STRING; 223926.28808408; -.
DR   EnsemblBacteria; BAC61613; BAC61613; BAC61613.
DR   GeneID; 1190958; -.
DR   KEGG; vpa:VPA0270; -.
DR   PATRIC; fig|223926.6.peg.3222; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_2_6; -.
DR   OMA; QARISYG; -.
DR   Proteomes; UP000002493; Chromosome 2.
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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   CHAIN           18..223
FT                   /note="Flagellar L-ring protein 2"
FT                   /id="PRO_0000009479"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00415"
SQ   SEQUENCE   223 AA;  24389 MW;  0E521AC89A6A4A03 CRC64;
     MKWLSKSWAV AVVLLVGCAG RQEFIPPQPN AEEYAPPKLD YTLPDAQSGS LYRHQYTMTL
     FQDRRAYRVG DVLTVVLSEE TSSSKKAGTK FGKSSAVNFA APTIGTKKFD ELGVSIDGSR
     NFDGSASSSQ GNKLQGAITV TVHDVLPNGV LRISGEKWLR LNQGDEFIRL TGIVRVDDIT
     RNNQVSSQRI ADARITYAGR GALADSNAAG WLTQFFNSPW VPF