ID A0A167ISN6_9SPHN Unreviewed; 365 AA.
AC A0A167ISN6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=A3736_09345 {ECO:0000313|EMBL:KZY55871.1};
OS Erythrobacter sp. HI0063.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY55871.1, ECO:0000313|Proteomes:UP000077326};
RN [1] {ECO:0000313|EMBL:KZY55871.1, ECO:0000313|Proteomes:UP000077326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0063 {ECO:0000313|EMBL:KZY55871.1,
RC ECO:0000313|Proteomes:UP000077326};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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:KZY55871.1}.
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DR EMBL; LWFF01000275; KZY55871.1; -; Genomic_DNA.
DR RefSeq; WP_067682175.1; NZ_LWFF01000275.1.
DR AlphaFoldDB; A0A167ISN6; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000077326; 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:KZY55871.1};
KW Cilium {ECO:0000313|EMBL:KZY55871.1};
KW Flagellum {ECO:0000313|EMBL:KZY55871.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077326};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 23..365
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009001434"
SQ SEQUENCE 365 AA; 37584 MW; 397434479B98226D CRC64;
MIRKLLIVLA AIAAVMPVPA MAERVRDLGQ FHSVRSNQLT GYGIVVGLDG SGDDNFAYLT
QAMRGVSGRL GLQLPPGVNP ALKNAAAVII TAELPAFAKP GQRIDVTVST MGKAKSLRGG
ALIMTPLYGA DGQVYAMAQG NLAVGGLGVS GQDGSKLTVN VPTVGRIADG ATVEAAVASN
FDFSEVLRWN LFQADFMTMT RVRDAINAAY PGMARIEDGV TLALAMPTGA DTRAGLMANI
EMLDVSPAER AAKVVINSRT GTIVISSAVR LAPAAISHGS LVVRIDENPQ IVQPAPFANG
QTAIEDDTTI TARQEGSYVT GIGPGASLAE VVDALNALGA SPADLVAILE GLKQAGSLTA
ELVII
//
