FLGI1_BRADU
ID FLGI1_BRADU Reviewed; 374 AA.
AC Q89I01;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Flagellar P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE AltName: Full=Basal body P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE Flags: Precursor;
GN Name=flgI1 {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=blr5838;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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=BAC51103.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000040; BAC51103.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_772478.1; NC_004463.1.
DR RefSeq; WP_028173283.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89I01; -.
DR SMR; Q89I01; -.
DR STRING; 224911.27354115; -.
DR EnsemblBacteria; BAC51103; BAC51103; BAC51103.
DR GeneID; 64025606; -.
DR KEGG; bja:blr5838; -.
DR PATRIC; fig|224911.44.peg.5784; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_5; -.
DR InParanoid; Q89I01; -.
DR OMA; VGPRDMI; -.
DR Proteomes; UP000002526; 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; 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..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 30..374
FT /note="Flagellar P-ring protein 1"
FT /id="PRO_0000041787"
SQ SEQUENCE 374 AA; 38942 MW; B12883FE5C128BB0 CRC64;
MPGVRWVRIV GVACAALSAL ALSVTSASAT SRIKDLANIE GVRQNQLIGY GLVVGLNGTG
DTLNNIPFTK QSLQAMLERM GVNIRGATIR TGNVAAVMVT GNLPAFATQG TRMDVTVSAL
GDAKNLQGGT LLVTPLLGAD GNVYAVAQGS LAISGFQAEG EAAKIVRGVP TVGRIANGAI
IEREIEFALN RLPNVRLALR NADFTTAKRI AAAVNDYLGV KTAEPIDPST VQLSIPPEFK
GNVVAFLTEI EQLQVDPDLA AKIVIDERSG IIVMGRDVRV ATVAVAQGNL TVTISESPQV
SQPNPLSRGR TVVAPRSSVS VTEDGRKLAL VKDGVSLQQL VDGLNGLGIG PRDMISILQA
IKAAGAIEAD IEVM