ID A0A3M0CH49_9PROT Unreviewed; 382 AA.
AC A0A3M0CH49;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=BXY39_1601 {ECO:0000313|EMBL:RMB08954.1};
OS Eilatimonas milleporae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC Kordiimonadaceae; Eilatimonas.
OX NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB08954.1, ECO:0000313|Proteomes:UP000271227};
RN [1] {ECO:0000313|EMBL:RMB08954.1, ECO:0000313|Proteomes:UP000271227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB08954.1,
RC ECO:0000313|Proteomes:UP000271227};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-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|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:RMB08954.1}.
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DR EMBL; REFR01000010; RMB08954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0CH49; -.
DR InParanoid; A0A3M0CH49; -.
DR OrthoDB; 9786431at2; -.
DR Proteomes; UP000271227; 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:RMB08954.1};
KW Cilium {ECO:0000313|EMBL:RMB08954.1};
KW Flagellum {ECO:0000313|EMBL:RMB08954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271227};
KW Signal {ECO:0000256|HAMAP-Rule:MF_00416}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT CHAIN 35..382
FT /note="Flagellar P-ring protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00416"
FT /id="PRO_5018342622"
SQ SEQUENCE 382 AA; 40518 MW; 996C1BD15DA2EFEC CRC64;
MNSVHKSGHT YTARVCFFLL MAVSVLLPVS TAMAVPTRLK DIISIEGVRD NQLVGYGLVV
GLDRSGDIIL NTPYTEQSIN AMLERLGINT KGRIQRGQNV AAVMVTATLP AFARQGTRID
VSIGSIGDAQ DLKGGILLAT PLLGADGEVY AVAQGGVAVA GFSAQGDAGS ITQGVPTSGR
IANGAIVERE VEFELSDLNT IKLSLHNPDL TTAQRIADKI NDHLGMFLSL PLDPATVQLN
RPVGYEKSLV QMLIDMERLE IEPDQRARVV IDERTGIIVM GSEVRINSVA IAQGNLTITI
SETPLVSQPA PFSEQGQTAI VPRTNIAIDD GSDRQLGILP PTVTLQELVD GLNALGVGPR
DMISILQAIK AAGAMQAELE VM
//
