ID A0A437JDH0_9SPHN Unreviewed; 374 AA.
AC A0A437JDH0;
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|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};
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=ENE74_01615 {ECO:0000313|EMBL:RVT43978.1};
OS Sphingobium algorifonticola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=2008318 {ECO:0000313|EMBL:RVT43978.1, ECO:0000313|Proteomes:UP000282977};
RN [1] {ECO:0000313|EMBL:RVT43978.1, ECO:0000313|Proteomes:UP000282977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLA-22 {ECO:0000313|EMBL:RVT43978.1,
RC ECO:0000313|Proteomes:UP000282977};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT43978.1}.
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DR EMBL; RZUL01000001; RVT43978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437JDH0; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000282977; 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:RVT43978.1};
KW Cilium {ECO:0000313|EMBL:RVT43978.1};
KW Flagellum {ECO:0000313|EMBL:RVT43978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282977}.
SQ SEQUENCE 374 AA; 38175 MW; CBB3FFFB2D9D1660 CRC64;
MTRTSNLFLK AIGVLVCLIA AIAFMPQARA ERIKDLGTFQ GVRPNQLTGY GLVVGLAGTG
DDAIQYATEG MKGVAARFGL TLPQGVNPAL KNAAAVLITA ELPAFSKPGQ RLDVTVSALG
KAKSLRGGTL ILSPLRGADG QIYAMAQGNL AVGGLGVSGA DGSQVSVNVP SAGRIPGGAT
VEQAVATGFD TAPTLTFNLA EADLTTALRV ADGINRAFGD RRARAMDAVS VTIDAAQGAE
ERILMMGLIE NIEIKPAEAP ARVIVNARTG TVVINGAVRI APAAVAHGKL TVSVKESPTV
VQPAPFSQGQ TAVEQSSTIN VDEERRPVID FKGGASLADI VKAVNAIGAS PADLVEILGA
LKQAGAMKAE LVVL
//
