ID   FLGI2_HAHCH             Reviewed;         378 AA.
AC   Q2SDU5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Flagellar P-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein 2 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI2 {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=HCH_04475;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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_00416}.
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_00416}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00416}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000155; ABC31179.1; -; Genomic_DNA.
DR   RefSeq; WP_011398246.1; NC_007645.1.
DR   AlphaFoldDB; Q2SDU5; -.
DR   SMR; Q2SDU5; -.
DR   STRING; 349521.HCH_04475; -.
DR   EnsemblBacteria; ABC31179; ABC31179; HCH_04475.
DR   KEGG; hch:HCH_04475; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000238; Chromosome.
DR   GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00416; FlgI; 1.
DR   InterPro; IPR001782; Flag_FlgI.
DR   PANTHER; PTHR30381; PTHR30381; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           34..378
FT                   /note="Flagellar P-ring protein 2"
FT                   /id="PRO_0000236303"
SQ   SEQUENCE   378 AA;  39105 MW;  DA139739D87A2DC5 CRC64;
     MHEVSDKTNA IHPLQRVSRA LFALGLLCFA AMAGAERIKD IATVEGVRSN QIVGYGLVVG
     LDGTGDKAPF TDQTFRNMMN RFGITIPAGT DPKLKNVAAV SVHADLPAFS KPGQKIDITV
     SSVGNAKSLR GGSLLMTNLK GADGKTYAVA QGNLVVGGFG AGGADGSSIT VNVPSVGRIP
     NGATVERAVP SSFSHGDTLT LNLSSPDFTT AKRVQDRIND LLGPGLAQAV DAASIRVMAP
     REASQRVGFL SILENLEVEP GQEAAKIVIN SRTGTIVVGQ NVKVLPAAVT HGNLTVTITE
     DFGVSQPNAL AGGDTVVVPQ TDVNVEQEPS RMFKFGPAAT LNDIVRAVNQ VGAAPGDVMA
     VLEALKQAGA LKAELIVI