ID A0A2T7UTH3_9RHOB Unreviewed; 366 AA.
AC A0A2T7UTH3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ECO:0000313|EMBL:PVE47962.1};
GN ORFNames=DDE23_07400 {ECO:0000313|EMBL:PVE47962.1};
OS Pararhodobacter aggregans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE47962.1, ECO:0000313|Proteomes:UP000244810};
RN [1] {ECO:0000313|EMBL:PVE47962.1, ECO:0000313|Proteomes:UP000244810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-19 {ECO:0000313|EMBL:PVE47962.1,
RC ECO:0000313|Proteomes:UP000244810};
RX PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA Foesel B.U., Drake H.L., Schramm A.;
RT "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT biofilter of a marine aquaculture.";
RL Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE47962.1}.
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DR EMBL; QDDR01000003; PVE47962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7UTH3; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000244810; 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:PVE47962.1};
KW Cilium {ECO:0000313|EMBL:PVE47962.1};
KW Flagellum {ECO:0000313|EMBL:PVE47962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244810};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 20..366
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5015789832"
SQ SEQUENCE 366 AA; 37561 MW; 591839376D2A249D CRC64;
MLRALAALLL ILLTASAAAA QIRLKDLVEF DGVRGNDLIG YGLVVGLDGT GDGIRNAPFT
EDIMTNILER LGVNITGEQF RPRNVAAVLV TATLPPFSRA GSRVDVTVSA IGDASSLFGG
TLVMTPLNGA DGQIYAVAQG AVLAGGVAAR GAAAQVVEGV PTSGSIPGGA RVEREVDFTL
ASLPRVRLAL RQADFTTAVR IEQVINSHFG RAVAAMQDSG TVLLDIAATR APSAAHALSQ
VENLVVDPGS RARVVIDQRS GTIVMGEDVR ISRVAVAQGG LTLRVEETPQ AIQPNPFSPG
ETVVVPRTNA SITPRPGVGM AEVAGGTSLA QVVAGLNALG VGPRDMIDIL NTINAAGALH
ADLVVR
//
