ID   A0A1I2JMY4_9GAMM        Unreviewed;       376 AA.
AC   A0A1I2JMY4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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};
GN   Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN   ORFNames=SAMN04488120_10899 {ECO:0000313|EMBL:SFF55488.1};
OS   Fontimonas thermophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Fontimonas.
OX   NCBI_TaxID=1076937 {ECO:0000313|EMBL:SFF55488.1, ECO:0000313|Proteomes:UP000199771};
RN   [1] {ECO:0000313|EMBL:SFF55488.1, ECO:0000313|Proteomes:UP000199771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23609 {ECO:0000313|EMBL:SFF55488.1,
RC   ECO:0000313|Proteomes:UP000199771};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOOC01000008; SFF55488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2JMY4; -.
DR   STRING; 1076937.SAMN04488120_10899; -.
DR   OrthoDB; 9786431at2; -.
DR   Proteomes; UP000199771; 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:SFF55488.1};
KW   Cilium {ECO:0000313|EMBL:SFF55488.1};
KW   Flagellum {ECO:0000313|EMBL:SFF55488.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199771}.
SQ   SEQUENCE   376 AA;  38527 MW;  659322F0883B8466 CRC64;
     MDRRACRFGS LPRLLCALLL VVQVVPGRAE RIKDLAAIQG VRGNPLVGYG LVVGLDGTGD
     QTTQAPFTTQ SLKAMLSQLG VVVPPNVNPQ LKNVAAVAVH AELPAFAKPG QAIDVTVSSI
     GNAGSLRGGS LLMTPLKGAD GQVYAIAQGN VIVGGLGVSG QDGSRVSINV PSAGRIPGGA
     LVERTVPNGF AAATELKLNL HTPDFTTAAR LAQAINTTLQ GDYAQALDAV TVAVRPPADP
     NQRVAFVGAL ENIEVTPGEA PARVVVNSRT GTVVIGSHVR VLPAAVAHGS LAVTISEKPR
     VSQPAPFSDG QTVVVPNTAI EVTQQGQGHM FLFESGVSLD DIVRAVNQVG AAPGDLVAIL
     EALRQAGALR AELVVI
//