ID A0A1B6YH44_9RHOB Unreviewed; 371 AA.
AC A0A1B6YH44;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:OAN67527.1};
GN ORFNames=A8B83_04680 {ECO:0000313|EMBL:OAN67527.1};
OS Rhodobacteraceae bacterium EhC02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN67527.1, ECO:0000313|Proteomes:UP000078223};
RN [1] {ECO:0000313|EMBL:OAN67527.1, ECO:0000313|Proteomes:UP000078223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC02 {ECO:0000313|EMBL:OAN67527.1,
RC ECO:0000313|Proteomes:UP000078223};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN67527.1}.
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DR EMBL; LXYH01000045; OAN67527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6YH44; -.
DR STRING; 1849170.A8B83_04680; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000078223; 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:OAN67527.1};
KW Cilium {ECO:0000313|EMBL:OAN67527.1};
KW Flagellum {ECO:0000313|EMBL:OAN67527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078223};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 28..371
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009004042"
SQ SEQUENCE 371 AA; 38653 MW; 1456E179C76FA7CE CRC64;
MRHSKRLIAT LVAIALAVGS APAPVQADVR IKDIAVFEGV RENQLVGYGL VVGLNGTGDR
LRNSPFTQRS IEGMLERLGV GNLSNETMRT ENTAAVMVTA MLPPFARRGS TIDVVVSSLG
DASSLRGGTL IVTPLAGADG AVYAVAQGPI AVAGYAAQGI NASIVEGVPT VARIENGATV
ENEVELAFNS LNSIRIALRT PDFTTAARVE EAINRSVGPG SAIALDPGTV EVRPNGKADI
FGLMSQIESL RVEPDSIAKV VIDARSGTIV IGSEVRIANV AVSQGGLTVI VREEIEVSQP
EPFSIGETVV VPQTNVQVQE RETQFTVLEG DVSLQRLVDG LNAIGLGATQ TISILQAIKA
AGALHADLEI I
//
