ID   A0A1X7AQH2_9GAMM        Unreviewed;       371 AA.
AC   A0A1X7AQH2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Flagellar P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI_2 {ECO:0000313|EMBL:SMA49657.1};
GN   Synonyms=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN   ORFNames=EHSB41UT_03439 {ECO:0000313|EMBL:SMA49657.1};
OS   Parendozoicomonas haliclonae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Parendozoicomonas.
OX   NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA49657.1, ECO:0000313|Proteomes:UP000196573};
RN   [1] {ECO:0000313|EMBL:SMA49657.1, ECO:0000313|Proteomes:UP000196573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA49657.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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_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:0000256|HAMAP-Rule:MF_00416}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|HAMAP-Rule:MF_00416}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000256|ARBA:ARBA00008994,
CC       ECO:0000256|HAMAP-Rule:MF_00416}.
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DR   EMBL; FWPT01000008; SMA49657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7AQH2; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000196573; Unassembled WGS sequence.
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; FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI; 1.
DR   PANTHER; PTHR30381:SF0; FLAGELLAR P-RING PROTEIN; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143, ECO:0000256|HAMAP-
KW   Rule:MF_00416}; Cell projection {ECO:0000313|EMBL:SMA49657.1};
KW   Cilium {ECO:0000313|EMBL:SMA49657.1};
KW   Flagellum {ECO:0000313|EMBL:SMA49657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196573};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT   CHAIN           26..371
FT                   /note="Flagellar P-ring protein"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT                   /id="PRO_5013413298"
SQ   SEQUENCE   371 AA;  38642 MW;  07FAA4BFA0663AD2 CRC64;
     MNRIIPVFLG LLLALSPFVS GPAQARRLMD LVDIQGVRTN QLIGYGLVVG LDGSGDKTRQ
     TEFTGQSLTN MLRQLGIQLP EDANPNLKNV AAVSVTATLP AFARPGQQID ITVSSIGDAK
     SLNGGTLLLT PLKGVDGNVY ALAQGNLVVS GISVSGGSGS EVTINVPTVG RIPSGAVIER
     SVATSFNDTG NVVLHLREPS FSNARNLARV INELLGPETA VANDGVSISV AAPKDSHQRV
     SYMAMLENLE VDTVRPPARV VINSRTGTVV MNEDVMVTPA AVSHGNLVVS IQESSTVSQP
     GAFSPGQTVT TPESNIQVQQ GEGRLFTVPE STSLQEVVNA LNSVGVTPAD LMAVLQALKQ
     AGSLKAELVV I
//