FLGI_BURPS
ID FLGI_BURPS Reviewed; 389 AA.
AC Q63YB1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Flagellar P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=BPSL0277;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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:0000255|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:0000255|HAMAP-Rule:MF_00416}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC Rule:MF_00416}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH34265.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; BX571965; CAH34265.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q63YB1; -.
DR SMR; Q63YB1; -.
DR STRING; 272560.BPSL0277; -.
DR EnsemblBacteria; CAH34265; CAH34265; BPSL0277.
DR KEGG; bps:BPSL0277; -.
DR eggNOG; COG1706; Bacteria.
DR OMA; KTIQITR; -.
DR Proteomes; UP000000605; Chromosome 1.
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; PTHR30381; 1.
DR Pfam; PF02119; FlgI; 1.
DR PRINTS; PR01010; FLGPRINGFLGI.
PE 3: Inferred from homology;
KW Bacterial flagellum; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 34..389
FT /note="Flagellar P-ring protein"
FT /id="PRO_0000041790"
SQ SEQUENCE 389 AA; 39623 MW; AB771142F5E8CEB7 CRC64;
MRPLVAARRR AAACCALAAC MLALAFAPAA ARAERLKDLA QIQGVRDNPL IGYGLVVGLD
GTGDQTMQTP FTTQTLANML ANLGISINNG SANGGGSSAM TNMQLKNVAA VMVTATLPPF
ARPGEAIDVT VSSLGNAKSL RGGTLLLTPL KGADGQVYAL AQGNMAVGGA GASANGSRVQ
VNQLAAGRIA GGAIVERSVP NAVAQMNGVL QLQLNDMDYG TAQRIVSAVN SSFGAGTATA
LDGRTIQLTA PADSAQQVAF MARLQNLEVS PERAAAKVIL NARTGSIVMN QMVTLQNCAV
AHGNLSVVVN TQPVVSQPGP FSNGQTVVAQ QSQIQLKQDN GSLRMVTAGA NLADVVKALN
SLGATPADLM SILQAMKAAG ALRADLEII
