ID A0A3A1P583_9SPHN Unreviewed; 366 AA.
AC A0A3A1P583;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=D2V17_17520 {ECO:0000313|EMBL:RIV81345.1};
OS Aurantiacibacter xanthus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1784712 {ECO:0000313|EMBL:RIV81345.1, ECO:0000313|Proteomes:UP000265366};
RN [1] {ECO:0000313|EMBL:RIV81345.1, ECO:0000313|Proteomes:UP000265366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2015396 {ECO:0000313|EMBL:RIV81345.1,
RC ECO:0000313|Proteomes:UP000265366};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-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:RIV81345.1}.
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DR EMBL; QXFM01000138; RIV81345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1P583; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000265366; 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:RIV81345.1};
KW Cilium {ECO:0000313|EMBL:RIV81345.1};
KW Flagellum {ECO:0000313|EMBL:RIV81345.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265366};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 24..366
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5017490853"
SQ SEQUENCE 366 AA; 37465 MW; B4BE7C8047EA5BCE CRC64;
MARLLALVAA AFVALGLAAP AQAERVRDLG AFQSVRSNQL TGYGIVVGLD GTGDDGFAYL
TQAMRGVSGR FGLQLPPGVN PALKNAAAVM ITADLPAFAK PGQRIDITVS TIGKAKSLRG
GALIMTPLYG ADGEIYAMAQ GNLAVGGLGV SGADGSSLTV NVPTVGRIPD GASVERAVAS
GFDADPILRF NLHQADFLTA SRVRDAINRR YPSIASVEDG VTLALRLPEG ADARASLMAD
IEMIPISPAE AAARVVVNSR TGTVVISSAV RLAPAAISHG SLVVRVEEDP MVVQPAPFSN
GRTAVEPDST ISVEQPANHI AMFDPGASLA EVVDALNALG ATPSDLVAIL EALKQAGSLK
AEMVVI
//
