ID A0A418X0G7_9BURK Unreviewed; 374 AA.
AC A0A418X0G7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 10.
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 {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=D3870_07845 {ECO:0000313|EMBL:RJG05941.1};
OS Noviherbaspirillum cavernae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320862 {ECO:0000313|EMBL:RJG05941.1, ECO:0000313|Proteomes:UP000285190};
RN [1] {ECO:0000313|EMBL:RJG05941.1, ECO:0000313|Proteomes:UP000285190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2R10-39 {ECO:0000313|EMBL:RJG05941.1,
RC ECO:0000313|Proteomes:UP000285190};
RA Zhu H.;
RL Submitted (SEP-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJG05941.1}.
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DR EMBL; QYUN01000002; RJG05941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418X0G7; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000285190; 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:RJG05941.1};
KW Cilium {ECO:0000313|EMBL:RJG05941.1};
KW Flagellum {ECO:0000313|EMBL:RJG05941.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285190};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 30..374
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5019594795"
SQ SEQUENCE 374 AA; 38446 MW; 2C0184D85508D630 CRC64;
MNISMPSVKR FLPILLGALC IAAAGSSHAE RLKDLASIQG VRQNQLMGYG LVVGLDGSGD
QTTQTPFTVQ SVVSMLQNMG VNLPPGASLQ LKNVAAVVVT SSLPAFAQPG QTLDVTVSSM
GNAKSLRGGT LVMTPLKGAD GQIYAMAQGN VVVGGVGASS AGSRTTINHL SVGRISAGAT
VERAVPTALG QDNMVQLELN DSDFSTASRV VDAINRRFGP DTASAQDGRV IRVRTPGSSD
ARVSFLGALE SLPVTPAQTA AKVILNARTG SVVMNQAVTL DSCAVSHGNL SVIINTENTP
SQPAPFSQGQ TVVTQNSQIE IKKEPGQVML LKAGTSLAEV VKALNAIGAT PQDLLAILQA
MKAAGSLRAE LEVI
//
