ID A0A1E2VEM9_9GAMM Unreviewed; 370 AA.
AC A0A1E2VEM9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=BFW38_12215 {ECO:0000313|EMBL:ODC05424.1};
OS Terasakiispira papahanaumokuakeensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Terasakiispira.
OX NCBI_TaxID=197479 {ECO:0000313|EMBL:ODC05424.1, ECO:0000313|Proteomes:UP000094291};
RN [1] {ECO:0000313|EMBL:ODC05424.1, ECO:0000313|Proteomes:UP000094291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH27A {ECO:0000313|EMBL:ODC05424.1,
RC ECO:0000313|Proteomes:UP000094291};
RA Seilhamer J.J.;
RL Submitted (AUG-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|ARBA:ARBA00008994,
CC ECO:0000256|HAMAP-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:ODC05424.1}.
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DR EMBL; MDTQ01000001; ODC05424.1; -; Genomic_DNA.
DR RefSeq; WP_069000445.1; NZ_MDTQ01000001.1.
DR AlphaFoldDB; A0A1E2VEM9; -.
DR STRING; 197479.BFW38_12215; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000094291; 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:ODC05424.1};
KW Cilium {ECO:0000313|EMBL:ODC05424.1};
KW Flagellum {ECO:0000313|EMBL:ODC05424.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094291};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 28..370
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5009353967"
SQ SEQUENCE 370 AA; 38347 MW; EF457AFFDE4A2CEF CRC64;
MKAFKIPARV CCLVALVVAA FAPLAQADRL KDITSVQGVR NNQLIGYGLV VGLNGTGDDA
PFTDQTFANM MTQFGITLPP GVNPDSENVA AVTVSAELPP FSKPGQAIDI TVSSIGNADS
LRGGTLLMTP LKGADGNTYA VAQGSLVVGG FGASGADGSK ITVNVPSVGR IPGGATVERS
IPNFFAKGDS LTLNLNYPDF TTARRVAEQI NDLMGPDVAQ ALDATSIRVR APRDSSQRVS
YLSVLENLEV DPAEAKARVI INSRTGTIII GQNVRVSPAA VTHGGLTVTI NENPQVSQPN
ALSDGDTTVT PQSQVNVQQG DGRMFKFDAG VTLDQLVQAV NQVGAAPGDL MAILEALKQA
GALKAELVVI
//
