ID A0A2N4YG45_9RHOB Unreviewed; 368 AA.
AC A0A2N4YG45;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=C0V75_14660 {ECO:0000313|EMBL:PLL12220.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL12220.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL12220.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL12220.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-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|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:PLL12220.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKRQ01000004; PLL12220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4YG45; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000234539; 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:PLL12220.1};
KW Cilium {ECO:0000313|EMBL:PLL12220.1};
KW Flagellum {ECO:0000313|EMBL:PLL12220.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234539};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 18..368
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5015014380"
SQ SEQUENCE 368 AA; 37326 MW; A1CF9CEE5B11C3EC CRC64;
MFLTLLLAVA LAPPASADRL KDIASVAGVR SNPLVGYGVV VGLSGTGDGN SGLTLQSLQS
LISRLGLTVE ASDLNARNAA AVMVTAELPP FMKEGQVLDV TVSTVGSAKS LKGGTLLMTP
LMGADGEIYA IAQGNLIVGG LGVEGQDGSS LTVNVPTVGR IPRGGTVERI VEAPFLDTES
LVLNLNRPDF STAAAVAKAI NEVFGPDIAT ALDGTSVAVR APYDANQRVT FMGMLENIEV
TPDAPAAKVV VNSRTGTVVI GGHVRVTPAA VTHGSLTVSI SEDPQVNQSA TVVNGDGTVV
VPGETTVTPD STITATEEAN RAFVFDPGVS LASLVDAINA VGASPSDLVA ILEALREAGA
LRAELVVI
//
