ID A0A1Y0G7E4_9PROT Unreviewed; 370 AA.
AC A0A1Y0G7E4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=CAP31_08350 {ECO:0000313|EMBL:ARU31692.1};
OS Sulfuriferula sp. AH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU31692.1, ECO:0000313|Proteomes:UP000195558};
RN [1] {ECO:0000313|EMBL:ARU31692.1, ECO:0000313|Proteomes:UP000195558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH1 {ECO:0000313|EMBL:ARU31692.1,
RC ECO:0000313|Proteomes:UP000195558};
RA Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT Duluth Complex.";
RL Submitted (MAY-2017) 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}.
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DR EMBL; CP021138; ARU31692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0G7E4; -.
DR KEGG; sulf:CAP31_08350; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000195558; Chromosome.
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:ARU31692.1};
KW Cilium {ECO:0000313|EMBL:ARU31692.1};
KW Flagellum {ECO:0000313|EMBL:ARU31692.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195558};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 26..370
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5013414147"
SQ SEQUENCE 370 AA; 38191 MW; 4D5563DC3426B7B2 CRC64;
MISWKLSLSL IFALLAMPLS GVAHADRLKD LASIQGVRQN QLIGYGLVVG LDGSGDQTTQ
TPFTVQSVAS MLKGMGVNLP PGTTLQLKNV AAVMVTSSLP AFAQPGQLLD VTVSSMGNAK
SIRGGTLLMT PLKGADGQIY AMAQGNVVVS GAGAAVNGAK AQINHLSVGR ISSGATVERA
VASALGQDNV IHLELNDTDF STASRVVDAI NQRFGKDTAA ALDGRVIQVR TPVGSNERVA
FLGNLESINV NPAQTIAKVI MNARTGSVVM NQSVTLDPCA VSHGNLSVVI KSEPSVSQPA
PFSRGKTTVT QSSQIEIKSE PGEMMMVKGG ASLSDVVKAL NAIGATPQDL LAILQAMKSA
GALRAELEII
//
