ID W8S0P5_9RHOB Unreviewed; 367 AA.
AC W8S0P5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Flagellar P-ring protein {ECO:0000256|ARBA:ARBA00019515, ECO:0000256|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000256|ARBA:ARBA00032344, ECO:0000256|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=roselon_01339 {ECO:0000313|EMBL:AHM03727.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM03727.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM03727.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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|HAMAP-
CC Rule:MF_00416}.
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DR EMBL; CP004372; AHM03727.1; -; Genomic_DNA.
DR RefSeq; WP_025311577.1; NZ_CP004372.1.
DR AlphaFoldDB; W8S0P5; -.
DR STRING; 1294273.roselon_01339; -.
DR KEGG; red:roselon_01339; -.
DR PATRIC; fig|1294273.3.peg.1316; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_5; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000019593; 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; 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:AHM03727.1};
KW Cilium {ECO:0000313|EMBL:AHM03727.1};
KW Flagellum {ECO:0000313|EMBL:AHM03727.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019593};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 21..367
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009024216"
SQ SEQUENCE 367 AA; 38123 MW; CDA4812160BFC5BB CRC64;
MSRFLSALLA LWLSLSMAMA MPVRIKDLVE FDGVRGNDLV GYGLVVGLNG TGDGLRNAPF
TEEIMVNILE RLGVNVTGEQ FRPQNVAAVI VTAELPPFAR QGGQIDVTVS AIGDADSLLG
GTLVMTPLTA ADGEIYAVAQ GAVIAGGASV EGDGASVVQG VPTAGVIPNG ARVEREIDFE
LASLSQVRLA LNSPDFTTAA RIEAAINHAF DRGVAVMLDA GTVLLDIGAT RAPSPAHALT
RVENILVEPE ARARVVVDQR SGTIVMGEDV RISRVAVAQG NLTLRIQEQP LAVQPNPFAD
GETVILPRTD ADIVEEPGTG LAEISGGTSL SEVVAALNAL GVSPREMIDI LSSIEAAGAL
HADFIVR
//
