ID A0A3S9Q9E1_9GAMM Unreviewed; 364 AA.
AC A0A3S9Q9E1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=EKO29_16950 {ECO:0000313|EMBL:AZQ85528.1};
OS Colwellia sp. Arc7-635.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2497879 {ECO:0000313|EMBL:AZQ85528.1, ECO:0000313|Proteomes:UP000286937};
RN [1] {ECO:0000313|EMBL:AZQ85528.1, ECO:0000313|Proteomes:UP000286937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arc7-635 {ECO:0000313|EMBL:AZQ85528.1,
RC ECO:0000313|Proteomes:UP000286937};
RA Lin J.;
RT "Complete Genome Sequences of Colwellia sp. Arc7-635, a Denitrifying
RT Bacterium Isolated from Arctic Seawater.";
RL Submitted (DEC-2018) 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|ARBA:ARBA00008994,
CC ECO:0000256|HAMAP-Rule:MF_00416}.
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DR EMBL; CP034660; AZQ85528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9Q9E1; -.
DR KEGG; cov:EKO29_16950; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000286937; 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:AZQ85528.1};
KW Cilium {ECO:0000313|EMBL:AZQ85528.1};
KW Flagellum {ECO:0000313|EMBL:AZQ85528.1};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 23..364
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5019596663"
SQ SEQUENCE 364 AA; 38098 MW; 71E6AECB063663B5 CRC64;
MKKYLYSFLC LTLLVFVPET NAQRIKDLAD VAGVRSNQLI GYGLVVGLPG TGEQSPFTEQ
SFKTMLSNFG IKMPDNLKPK IKNVAAVAVH AELPAFSKPG QRIDVTVSSM GSAQSLRGGT
LIQTILMGLD GNAYAVAQGS LIVSGLGAEG LDGSKVIANT PTVGRIANGA MVEREVLSPF
SSGDHITFNL HNADFTTAKR LSDTINNLIA GSARAIDAAS VKVTAPRDAA DRVSFLATLE
NLEFEPGSPS AKIIVNSRTG TIVIGADVRL LPAAITHGGI TVTINELANV SQPNAFAEGE
TVATNQSIID VKQDDSRMFV FNPGVTLDAL VRAINQVGAG PGDVMAILEA LDQAGALRGD
LIII
//
