ID A0A0Q5PM10_9BURK Unreviewed; 374 AA.
AC A0A0Q5PM10;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Flagellar P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein {ECO:0000256|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI {ECO:0000256|HAMAP-Rule:MF_00416};
GN ORFNames=ASG35_30050 {ECO:0000313|EMBL:KQR82436.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR82436.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR82436.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR82436.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR82436.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR82436.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR82436.1}.
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DR EMBL; LMPF01000011; KQR82436.1; -; Genomic_DNA.
DR RefSeq; WP_056356423.1; NZ_LMPF01000011.1.
DR AlphaFoldDB; A0A0Q5PM10; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000051826; 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:KQR82436.1};
KW Cilium {ECO:0000313|EMBL:KQR82436.1};
KW Flagellum {ECO:0000313|EMBL:KQR82436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 27..374
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5008994284"
SQ SEQUENCE 374 AA; 38439 MW; B09A6006CE0EA6C7 CRC64;
MKFALRFCFG ALALALAAVL PQAAQAERLK DLVSFQGVRD NQLIGYGLVV GLDGTGDQTS
QTPFTTQSLT NMLGNLGITL NPATTQNMQL KNVAAVMVTA VLPPFARPGE AIDVTVSSLG
NAKSLRGGTL LMAPLKGADG QVYAMAQGNV VIGGAGASAN GSKVQVNSLG AGRISGGALV
ERAVPSNFTQ PGGTMQMELR DMDFDNAQKI VAAVNNQFGM GTAVALDGRT IQLHAPTDPT
SQVSFMAQLE NIDVRPSQAA AKVILNARTG SIVMNQMVTL QNCAVAHGNL SVVINTQTAV
SQPGAFSNGQ TVAARQSNIQ LKQDSGALKT VAASATLAEV VKALNALGAT PADLISILQS
MKAAGALRAD LEII
//
