ID A0A1H8LRV8_9RHOB Unreviewed; 370 AA.
AC A0A1H8LRV8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
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 ORFNames=SAMN04490248_101266 {ECO:0000313|EMBL:SEO07819.1};
OS Salinihabitans flavidus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salinihabitans.
OX NCBI_TaxID=569882 {ECO:0000313|EMBL:SEO07819.1, ECO:0000313|Proteomes:UP000198893};
RN [1] {ECO:0000313|EMBL:SEO07819.1, ECO:0000313|Proteomes:UP000198893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27842 {ECO:0000313|EMBL:SEO07819.1,
RC ECO:0000313|Proteomes:UP000198893};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FODS01000001; SEO07819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8LRV8; -.
DR STRING; 569882.SAMN04490248_101266; -.
DR Proteomes; UP000198893; 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:SEO07819.1};
KW Cilium {ECO:0000313|EMBL:SEO07819.1};
KW Flagellum {ECO:0000313|EMBL:SEO07819.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198893};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 24..370
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5011803950"
SQ SEQUENCE 370 AA; 38695 MW; E3AA94CD07765423 CRC64;
MNETFRMLAT VLCTLLLAGS ATANQIRIKD LVEFDGVRGN DLLGYGLVVG LNGSGDGLRN
APFTEEIMSN TLERLGVNVS GEQFRPKNVA AVLVTAALPP FARAGGRIDV TVSAIGDAKS
LLGGTLVMTP LNAADGRIYA VAQGTVIAGG AAAQGDAGGV VQGVPTAGVI PAGARVEREI
EFDFTSLTSL RLALREPDFT TAARIERAIN RDFGRGVSVM LDAGTVHLDI AATQSRSPAH
ALGRVENILV QPERKARVVV DQRSGTIVMG DDVRISRVAV SQGNLTIRIQ ERPLAVQPNP
FSDGRTVVVP RTDAEIIEEE GVGLAEVPEG ASLSEVVAGL NALGVAPRDM IDILKSIKAA
GALHAEFLVR
//
